REFR
{
RETE|ID 1 FBrf0144466	AU 1 Adolfsen et al.	YR 1 2001	TP 1 Abstract	TI 1 Characterization of the Drosophila synaptotagmin family.	REFM 1 Bellen, Taylor, 2001: 18		
ID|FBrf0144466
TP|abstract
|Drosophila meeting abstract
MABST|A mechanistic understanding of how synaptic calcium signals are transduced
| into membrane fusion and neurotransmitter release is largely unknown.
| Biochemical and genetic studies on synaptotagmin I are consistent with the
| idea that synaptotagmin I is a major calcium sensor at synapses, although
| it likely plays multiple roles in vesicle cycling. Currently, 12
| synaptotagmin isoforms have been isolated in mammals, and six to eight
| homologues have been found in Drosophila and C. elegans. Outside of
| synaptotagmin I the function of the remaining synaptotagmins is unknown. We
| are interested in characterizing the localization, biochemistry and
| function of the Drosophila synaptotagmin family. Among the Drosophila C2
| family, eight proteins are most homologous to synaptotagmins. These include
| homologs of mammalian isoforms I, IV, VII, IX, V/ X, Srg-1, and two
| additional synaptotagmin-like proteins. Of these, only the synaptotagmin IX
| homolog lacks the a transmembrane domain. In addition, Drosophila contains
| a number of synaptotagmin-related proteins including one tricalbin homolog,
| one granuphilin homolog and one otoferlin homolog. Other C2-domain
| containing proteins include one Rabphilin homolog, one RIM homolog, three
| proteins with some homology to Munc-13, and four additional novel
| C2-containing proteins. We have generated antisera against the immediate
| synaptotagmin family and have initiated studies to determine the cellular
| and subcellular distribution of each isoform. We have also begun a
| biochemical analysis of the family to determine their calcium-dependent
| properties and protein-protein interactions. We will present our findings
| on the localization and biochemical properties of the Drosophila
| synaptotagmin family that will facilitate our subsequent genetic analysis
| to determine the function of the neuronal expressed isoforms.
AU|Adolfsen
|B.
AU|Mikula
|M.
AU|Littleton
|J.T.
YR|2001
TI|Characterization of the Drosophila synaptotagmin family.
JR|Bellen, Taylor, 2001
PG|18
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144467	AU 1 Almeida et al.	YR 1 2001	TP 1 Abstract	TI 1 Investigating the role of Notch and grainyhead in the post embryonic neuroblasts.	REFM 1 Bellen, Taylor, 2001: 180		
ID|FBrf0144467
TP|abstract
|Drosophila meeting abstract
MABST|Neuroblasts are the precursors, which give rise to the differentiated cells
| of the nervous system. In Drosophila, after the first stage of neurogenesis
| is complete in the late embryo, all but two of the neuroblasts (NBs) cease
| dividing. Many of the NBs then become dormant, whilst a few disappear,
| probably undergoing programmed cell death. The dormant NBs are reactivated
| in late second instar. They then proliferate producing clusters of progeny
| that contribute to the adult nervous system at metamorphosis. The larval
| postembryonic neuroblasts (pNBs) therefore have characteristics of neural
| stem cells since they have the ability to self-renew and to generate
| progeny that will contribute to the adult nervous system. Our interest in
| the pNBs has come from two directions. First we know that the Notch pathway
| is active in the pNB lineages, but we cannot easily reconcile this activity
| with known functions of Notch at other stages of neurogenesis. Second, we
| have been studying a gene, grainyhead which is expressed in the pNBs. We
| are now investigating the role of both genes, taking advantage of a pNB
| enhancer from grainyhead that allows us to manipulate gene expression in
| these cells. Our preliminary results from these analyses will be presented.
AU|Almeida
|M.
AU|Harrison
|E.
AU|Bray
|S.
YR|2001
TI|Investigating the role of Notch and grainyhead in the post embryonic neuroblasts.
JR|Bellen, Taylor, 2001
PG|180
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144468	AU 1 Arruda and Dolph	YR 1 2001	TP 1 Abstract	TI 1 An allele of pawn that disrupts phototransduction in Drosophila.	REFM 1 Bellen, Taylor, 2001: 119		
ID|FBrf0144468
TP|abstract
|Drosophila meeting abstract
MABST|We have isolated a novel mutation with dramatic effects on
| phototransduction. Mutant flies exhibit a novel electrophysiological
| response to light with high-frequency oscillations during photoreceptor
| cell depolarization. The allele also exhibits a rapid light-dependent
| retinal degeneration that appears unlike any that has been previously
| documented where microvilli are selectively lost from the distal tips of
| the rhabdomeres. In addition, there are several morphological traits
| associated with this allele, including, embryonic lethality, truncated
| bristles, and black melanic deposits on the eyes of mutant flies.
| Interestingly, mutations in the pawn gene share the lethality, bristle, and
| eye phenotypes however, these flies have neither the ERG nor the retinal
| degeneration phenotypes. Genetic data has demonstrated that our mutation is
| a new allele of pawn (pawn 14S7 ). Genetic and PCR analysis allowed us to
| map the molecular lesion to be a deletion in the CG11101 ORF resulting in a
| premature stop codon. In addition, three different pawn alleles were
| determined to have point mutations within this same coding region. CG11101
| is a single -pass transmembrane protein with a large extracellular domain
| and small cytoplasmic tail. Proteins with this architecture are classified
| as cell adhesion molecules. Data will be presented which suggests that the
| retinal degeneration and oscillating electroretinogram phenotypes
| characteristic of pawn 14S7 are due to the misexpression of the truncated
| Pawn product disrupting a vital process involved in phototransduction.
AU|Arruda
|S.E.
AU|Dolph
|P.J.
YR|2001
TI|An allele of pawn that disrupts phototransduction in Drosophila.
JR|Bellen, Taylor, 2001
PG|119
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144469	AU 1 Ghezzi et al.	YR 1 2001	TP 1 Abstract	TI 1 Transcriptional modulation of the Drosophila slowpoke gene after acute exposure to solvent anesthetics.	REFM 1 Bellen, Taylor, 2001: 19		
ID|FBrf0144469
TP|abstract
|Drosophila meeting abstract
MABST|Electrically excitable cells depend on the activity of ion channels to
| transmit information by means of electrical impulses. To efficiently convey
| information, the ion channel protein density must be tailored to the
| demands of the existing environment. An increase in channel density can
| have a strong impact on the cellular electrical properties. We have
| observed that exposure of the fruit fly Drosophila melanogaster to benzyl
| alcohol, an anesthetic that induces a hyperexcitable behavior, causes an
| increase in the mRNA abundance of the Ca2+ activated K+ channel, slowpoke
| (slo). Message abundance was measured by Ribonuclease Protection Assay.
| However, to determine whether the increase was the result of increased
| message stability or an increase in slo transcription we used a transgenic
| line that contains the slo neuronal promoter upstream of the
| b-galactosidase reporter gene. b-galactosidase levels were measured
| following acute treatment with benzyl alcohol. The observed increase in of
| b-galactosidase's specific activity is an indicator that the increase in
| slo mRNA is partially a result of a transcriptional response.
AU|Ghezzi
|A.
AU|Al-Hasan
|Y.M.
AU|Larios
|L.E.
AU|Atkinson
|N.S.
YR|2001
TI|Transcriptional modulation of the Drosophila slowpoke gene after acute exposure to solvent anesthetics.
JR|Bellen, Taylor, 2001
PG|19
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144470	AU 1 Awasaki and Ito	YR 1 2001	TP 1 Abstract	TI 1 Development of the clonal unit, lineage-related neural circuit module.	REFM 1 Bellen, Taylor, 2001: 146		
ID|FBrf0144470
TP|abstract
|Drosophila meeting abstract
MABST|The central brain of Drosophila melanogaster is produced by an average of 85
| stem cells (neuroblasts) per hemisphere. In order to assess the role of
| cell lineage in the neural circuit formation, we visualized the innervation
| patterns of the progeny of single neuroblasts in the adult brain using the
| FRT-GAL4 system. In the majority of clones identified so far, cell bodies
| form a tightly packed cluster. Their neurites fasciculate to form a single
| bundle and innervate a limited number of neuropile regions in a stereotypic
| manner. These suggest that, in many cases, the progeny of a single
| neuroblast form a lineage-dependent circuit module, which we named a
| "clonal unit". In the developing larval brain, clustering of clonal cell
| bodies and fasciculation of neurites are already apparent. To understand
| the mechanisms underlying this clonal clustering and fasciculation, we
| first focused on the role of neural-specific homophilic cell adhesion
| molecules in the cell body layer (cortex) of the developing larval brain.
| DN-cadherin and Neuroglian are distributed uniformly along the border
| between all the neurons. FasciclinII (FasII), on the other hand, localizes
| in several clusters of neurons, each of which looks like clonally related.
| Double labeling of FRT-GAL4 clones and FasII-expressing cells revealed that
| FasII clusters indeed correspond to clones. The distribution of FasII is
| limited to the cell border inside the clones. Cell surface flanking the
| neighboring clones is free of FasII. Such localization might infer that
| FasII would mediate cell-cell adhesion within clonal cluster. fasII mutant
| clones induced by the MARCM system, however, showed no remarkable defect on
| the formation of clonal cell clustering. Pan-neuronal ectopic expression of
| fasII, induced by the elav promoter, caused little effect, either. The
| ectopically expressed FasII, on the other hand, showed the same
| characteristic localization pattern: it concentrates along the intraclonal
| cell borders but not along the interclonal cell borders. Why doesn't
| ectopic FasII exist at the interclonal cell borders? One possible
| explanation is that there might be physical boundary that prevents direct
| contact of neurons between different clones. We thus examined the
| arrangement of glial cells in the larval brain. Double labeling of glial
| cells and FasII -expressing clones showed that a type of glia -cell body
| glial cells -send extensive processes between neurons. In the outer area of
| the cell body layer, which is near the brain surface and houses neuroblasts
| and newly generated cells, glial processes wrap only the outer surface of
| the clonal clusters. Processes are not observed within the cluster. Glial
| cells thus physically separate the clonal border in this area. Deeper in
| the cell body layer, which consists of old cells, thin glial processes
| penetrate the boundary between essentially all the neurons.
AU|Awasaki
|T.
AU|Ito
|K.
YR|2001
TI|Development of the clonal unit, lineage-related neural circuit module.
JR|Bellen, Taylor, 2001
PG|146
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144471	AU 1 Babcock and Pallanck	YR 1 2001	TP 1 Abstract	TI 1 A screen for synaptic transmission mutants in Drosophila.	REFM 1 Bellen, Taylor, 2001: 20		
ID|FBrf0144471
TP|abstract
|Drosophila meeting abstract
MABST|The fly compound eye is a powerful system for identifying and characterizing
| genes involved in signal transduction, synaptic transmission and
| neurodegeneration. Our lab is using the EGUF/ hid system (Stowers &
| Schwarz, 1999, Genetics 152, 1631) to conduct a screen for synaptic vesicle
| trafficking components that function in the photoreceptor presynaptic
| terminal. When used in a screening context, this system generates F1 mosaic
| offspring bearing photoreceptor cells that are homozygous for a particular
| mutagenized chromosome arm. We have used this system to screen 7500
| mutagenized chromosomes for defects conferring non-phototactic phenotypes.
| Characterization of 50 mutants recovered from this screen using
| electroretinogram recordings revealed five mutants with normal
| photoreceptor depolarization, but defective synaptic transmission. These
| mutants are currently being subjected to deficiency mapping, and further
| electrophysiological analysis at the neuromuscular junction. Results from
| these experiments will be presented.
AU|Babcock
|M.
AU|Pallanck
|L.
YR|2001
TI|A screen for synaptic transmission mutants in Drosophila.
JR|Bellen, Taylor, 2001
PG|20
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144472	AU 1 Baines et al.	YR 1 2001	TP 1 Abstract	TI 1 Fasciclin II regulates synaptic connetivity in the embryonic CNS.	REFM 1 Bellen, Taylor, 2001: 92		
ID|FBrf0144472
TP|abstract
|Drosophila meeting abstract
MABST|The mechanisms that underlie the formation of synaptic connections in the
| CNS are not well understood. It is conceivable, however, that molecules
| required for synaptic development at the more accessible peripheral
| neuromuscular junction (NMJ) may similarly contribute to synaptogenesis in
| the CNS. To test this, we have investigated the involvement of Fasciclin II
| (FasII), a key molecule involved in axonal guidance, target selection and
| synaptic plasticity at the Drosophila NMJ, in the development of identified
| synapses between cholinergic interneurons and glutaminergic motorneurons in
| the embryonic CNS. We will show that although the initial formation of
| synaptic connections between these neurons is independent of FasII, it is
| required for the subsequent elaboration of these connections during
| postembryonic development. To this extent therefore, the involvement of
| FasII in central synaptogenesis parallels that at the NMJ. Although FasII
| is not essential for the initial formation of central synapses in the
| embryo, asymmetric alterations in the level of its expression, induced via
| targeted transgene expression in either the pre or postsynaptic neuron( s),
| are sufficient to disrupt the formation of a normal pattern of embryonic
| synaptic connectivity. This effect is isoform specific, being observed only
| with expression of a transmembrane (TM) isoform, but not a glycosyl
| phosphatidyl inositol (GPI)-linked isoform of FasII. We link this
| specificity in effect to our observation that the relative abundance of
| mRNA encoding TM, but not GPI-linked, isoforms of FasII is influenced by
| blocking evoked neurotransmitter release in all neurons of the embryonic
| CNS. This latter finding implies that synaptic activity, acting through
| altered levels of FasII expression, may contribute to the establishment of
| a proper pattern of central synaptic connections during embryogenesis.
AU|Baines
|R.A.
AU|Seugnet
|L.
AU|Thompson
|A.
AU|Bate
|M.
YR|2001
TI|Fasciclin II regulates synaptic connetivity in the embryonic CNS.
JR|Bellen, Taylor, 2001
PG|92
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144473	AU 1 Yu et al.	YR 1 2001	TP 1 Abstract	TI 1 Regulation of effector and initiator caspases in the development of the Drosophila eye.	REFM 1 Bellen, Taylor, 2001: 3		
ID|FBrf0144473
TP|abstract
|Drosophila meeting abstract
MABST|Regulated cell death and survival play important roles in neural
| development. Seven apparent caspases are presumed to be regulated by
| extracellular signals to determine the final structure of the nervous
| system. We found that an antibody raised against a peptide from human
| caspase 3 crossreacts specifically with dying Drosophila cells, and used
| this reagent to investigate how extracellular signals control spatial
| patterning of cell death during eye development. The antibody labeled
| activated effector caspases DCP-1 and Drice. We show that the initiator
| caspase DRONC and the proapoptotic gene head involution defective (hid)
| were are important for DCP1/ Drice activation in vivo. We have evidence
| that DRONC may also play direct roles in addition to activating downstream
| effector caspases. EGFR, Notch, and intact primary pigment and cone cells
| have each been implicated in survival or death signals in the eye.
| Epistasis experiments ordered these three signals into a single pathway
| that affects caspase activity through Inhibitor-of-Apoptosis proteins
| (IAPs). None of these extracellular signals appeared to act by promoting
| caspase activation directly. Taken together, these findings indicate that
| spatial regulation of cell death and survival is integrated through a
| single pathway in eye development.
AU|Yu
|S.Y.
AU|Yoo
|S.J.
AU|Yang
|L.
AU|Zapata
|C.
AU|Srinivasan
|A.
AU|Hay
|B.A.
AU|Baker
|N.E.
YR|2001
TI|Regulation of effector and initiator caspases in the development of the Drosophila eye.
JR|Bellen, Taylor, 2001
PG|3
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144474	AU 1 Baker et al.	YR 1 2001	TP 1 Abstract	TI 1 Ciliogenesis mutations affect sensory neuron function.	REFM 1 Bellen, Taylor, 2001: 120		
ID|FBrf0144474
TP|abstract
|Drosophila meeting abstract
MABST|Dendritic outer segments, the probable sites of transduction in external
| sense organs and chordotonal organs, are modified cilia. While some
| mutations affecting mechanosensory response have identified components of
| the transduction machinery, others disrupt the development or structure of
| these modified cilia. Previously, it was shown that some mutations with
| defects in axoneme structure affected chordotonal cilia, but not the highly
| modified cilia in es organs (Eberl et al, 2000). Here we describe genes
| that act in all ciliated sensory neurons. One class, which appears to be
| required for the generation of a functional basal body from its antecedent
| centriole, includes the unc and nompJ mutations. In unc mutants the cilia
| of chordotonal organs and the flagella of spermatids are often broken or
| splayed. The basal bodies of these cells are disrupted. These flies also do
| not produce motile sperm, and show defects in nuclear reshaping and
| individualization. A functional GFP tagged version of the novel protein
| localizes to centrioles and centriole adjuncts during spermatogenesis and
| to basal bodies during sense organ development. We are working to identify
| functional domains by dissecting the 1386 AA protein. One construct,
| consisting of the amino-terminal 977 AA, localizes to centrioles during
| spermatogenesis, but does not rescue. A slightly shorter construct of 663
| AA does not localize or rescue. Surprisingly a UAS-construct containing the
| carboxy-terminal 723 amino acids can rescue the mutant phenotype. Although
| UNC-GFP is localized to centrioles at the earliest stages of
| spermatogenesis, meiosis is completed normally in unc mutants. By contrast,
| nompJ mutants show meiotic defects, indicating an earlier requirement for
| this gene product. Spermatids and spermatocytes in these flies also
| mislocalize UNC-GFP and gamma-tubulin. We are currently mapping nompJ and
| further defining the mutant phenotype. Members of the second class,
| typified by nompB, have defects in both chordotonal and bristle sensory
| cells. nompB flies do not produce the elongated ciliary outer-segments
| typical of chordotonal sensory neurons, and show a gap between the neuron
| and cuticular dome in campaniform sensilla. The probable nompB gene encodes
| the Drosophila homolog of IFT88/ OSM-5/ Polaris, a conserved protein
| expressed in ciliated cells from algae to mammals. Homologs are part of a
| protein complex that mediates transport to and from the tip of growing
| cilia and flagella. Interestingly, although the protein is required to
| construct a variety of cilia in these taxa, nompB mutations do not prevent
| the production of motile sperm in Drosophila: either fly sperm do not
| require IFT, or it is required after spermatogenesis. We are currently
| asking if nompB is needed for sperm function.
AU|Baker
|J.D.
AU|Han
|Y.G.
AU|Kernan
|M.
YR|2001
TI|Ciliogenesis mutations affect sensory neuron function.
JR|Bellen, Taylor, 2001
PG|120
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144475	AU 1 Hatzidakis et al.	YR 1 2001	TP 1 Abstract	TI 1 Characterization of fruitless-expressing cells and their role in male sexual behavior.	REFM 1 Bellen, Taylor, 2001: 105		
ID|FBrf0144475
TP|abstract
|Drosophila meeting abstract
MABST|The fruitless (fru) gene heads a branch of the sex determination hierarchy
| that builds the potential for male sexual behavior into Drosophila
| melanogaster. Transcripts from the 4 promoters of the fruitless gene encode
| BTB zinc-finger transcription factors. The transcripts from the most
| upstream fru promoter (P1) are sex-specifically spliced and it is the
| P1-derived products that are responsible for fru's role in male sexual
| behavior. Male flies null for the P1 encoded proteins do not court, whereas
| P1 hypomorphs show defects throughout the courtship sequence. The absence
| of P1-derived products in females has no apparent phenotype. The P1-derived
| products of fru are expressed in about 2% of the cells of the central
| nervous system (about 1700 cells). Most of these neurons are found in about
| 20 clusters of fruitless-expressing cells; the remainder appear as isolated
| cells. We want to understand the roles of the different clusters of
| fru-expressing cells in the different stages of male sexual behavior. To
| achieve this goal, we are currently isolating the enhancers of fruitless,
| expecting that different enhancers can be identified that drive expression
| in different subsets of fru-expressing cells. We have tested over 25
| fragments from across the 140 KB fru transcriptional unit for enhancer
| activity with the GAL4-UAS system. We are determining whether these genomic
| fragments can act as enhancers by their ability to drive the expression of
| UAS-GFP in subsets of the cells in which products of the P1 fru promoter
| are normally expressed. The characterization of one enhancer which governs
| the expression of fru in the optic lobes will be presented. We are studying
| the roles that these, and other fru-expressing cells have in male sexual
| behavior by using the GAL4-UAS system to sexually transform and to cause
| the apoptosis of subsets of these cells.
AU|Hatzidakis
|J.
AU|Reynaud
|E.
AU|Baker
|B.
YR|2001
TI|Characterization of fruitless-expressing cells and their role in male sexual behavior.
JR|Bellen, Taylor, 2001
PG|105
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144476	AU 1 Banerjee and Hasan	YR 1 2001	TP 1 Abstract	TI 1 A study of intracellular signaling underlying axon guidance.	REFM 1 Bellen, Taylor, 2001: 204		
ID|FBrf0144476
TP|abstract
|Drosophila meeting abstract
MABST|Genetic analysis in Drosophila has lead to the discovery of many genes
| involved in wiring of the embryonic central nervous system. Several studies
| have provided a detailed understanding of how axons are guided with respect
| to the midline (reviewed by Tear G., 1999). Some neurons cross the midline
| once and project contralaterally, while others always project
| ipsilaterally, away or along the midline. It is becoming increasingly
| evident that a balanced output, generated by preferential expression of
| cell surface receptors and selective activation of intracellular signaling
| pathways guide an axon towards the midline or away from it. In an effort to
| link known extracellular pathways to specific intracellular signaling
| molecules, we have studied the role of dgq in axon guidance. dgq codes for
| the a subunit of the Gq class of heterotrimeric G proteins. Overexpression
| of the activated form of Gqa can reroute FasII positive axons cross the
| midline ( Ratnaparkhi and Hasan., 2001). Subsequent analysis suggested that
| Gqa is involved in modulating the repulsive behavior of a neuron, possibly
| in response to attractive cues. It has recently been shown that Abl Kinase
| regulates Robo mediated repulsive signaling (Bashaw GJ et al., 2000). One
| likely but speculative, hypothesis is that Gqa modulates repulsive
| signaling through activation of one or more tyrosine kinases. We are
| presently studying a group of tyrosine kinases as putative interactors of
| Gqa. Results of these studies will be discussed. References: Bashaw GJ et
| al., Cell. 2000 Jun 23; 101( 7): 703-15 Ratnaparkhi A and Hasan G. 2001(
| submitted). Tear G. Trends Genet. 1999 Mar; 15( 3): 113-8. Review
AU|Banerjee
|S.
AU|Hasan
|G.
YR|2001
TI|A study of intracellular signaling underlying axon guidance.
JR|Bellen, Taylor, 2001
PG|204
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144477	AU 1 Barolo et al.	YR 1 2001	TP 1 Abstract	TI 1 Hairless recruits the co-repressors CtBP and Groucho to the Notch pathway activator suppressor of hairless during PNS development.	REFM 1 Bellen, Taylor, 2001: 1		
ID|FBrf0144477
TP|abstract
|Drosophila meeting abstract
MABST|Suppressor of Hairless [Su( H)] is a DNA-binding transcription factor,
| conserved from flies to humans, which interacts with the activated Notch
| receptor to activate target genes. Su( H) is a transcriptional activator in
| the presence of Notch signaling, but can act as a repressor in the absence
| of signaling. We have previously shown that this repressor activity is
| essential for proper cell fate specification in the mechanosensory bristle
| 1 . Hairless (H), a novel protein, binds to Su( H) and has been pr oposed
| to inhibit Notch signaling by inhibiting DNA binding by Su( H) 2 . We will
| present evidence for an alternative hypothesis: that H antagonizes Notch
| signaling by acting as an adaptor between Su( H) and the co-repressors
| C-terminal Binding Protein (CtBP) and Groucho, thereby mediating direct
| repression of Notch target genes. We find that mutations in both dCtBP and
| groucho (gro) enhance the effects of loss of H function and of Su( H)
| de-repression during mechanosensory bristle development. This role for gro
| is surprising, since it has not previously been found to antagonize Notch
| signaling--in fact, gro is traditionally classified as a neurogenic gene.
| We will also show that the H protein contains conserved motifs that
| resemble CtBP and Gro interaction domains, and will present evidence that H
| directly interacts with both co-repressors in vitro. Our proposed "adaptor"
| model for H function conflicts with previous work 2 which indicated that an
| excess of H can block DNA-binding by Su( H) in vitro. We will present
| evidence that at lower H concentrations, Su( H) can bind simultaneously to
| both H and DNA in vitro. We will also describe in vivo misexpression
| experiments in which H-VP16 fusions act oppositely to wild -type H, a
| result consistent with a co-repressor/ adaptor model for H but not easily
| reconciled with a DNA-binding inhibition model. Taken together, these
| findings suggest an unusual mechanism for Su( H) -mediated repression of
| Notch target genes during PNS development. 1 Barolo, S., et al. (2000).
| Cell 103: 957-69. 2 Brou, C., et al. (1994). Genes Dev. 8: 2491-503.
AU|Barolo
|S.
AU|Stone
|T.
AU|Medders
|K.
AU|Posakony
|J.W.
YR|2001
TI|Hairless recruits the co-repressors CtBP and Groucho to the Notch pathway activator suppressor of hairless during PNS development.
JR|Bellen, Taylor, 2001
PG|1
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144478	AU 1 Barros et al.	YR 1 2001	TP 1 Abstract	TI 1 Myosins and asymmetic neuroblast division.	REFM 1 Bellen, Taylor, 2001: 147		
ID|FBrf0144478
TP|abstract
|Drosophila meeting abstract
MABST|During the neuroblast cell cycle, differential subcellular targeting of
| protein complexes results in the asymmetric segregation of cell fate
| determinants, such as Prospero. We are investigating the mechanisms that
| underlie the dynamic localisation of determinants in dividing neuroblasts.
| The actin cytoskeleton appears to play a fundamental role in establishing
| neuroblast asymmetry, as disruption of actin filaments leads to
| mislocalisation of Prospero. Treatment of neuroblasts with general myosin
| inhibitors, such as BDM, suggest that actin-based motor proteins may also
| be involved in asymmetric cell division. Furthermore the tumour-suppressor
| protein, Lethal giant larvae, which binds to non-muscle myosin II, was
| shown recently to play a role in asymmetric segregation. We are studying
| the role of different myosins in asymmetric cell division. We have followed
| the dynamic distribution of myosin II in living embryos and find that it is
| asymmetrically localised in neuroblasts. By blocking myosin II activity, we
| have shown that myosin II is essential for the asymmetric localisation of
| Prospero, Staufen and Numb. We are using similar approaches to investigate
| the role of unconventional myosins in the establishment of neuroblast asymmetry.
AU|Barros
|C.
AU|Phelps
|C.B.
AU|Brand
|A.H.
YR|2001
TI|Myosins and asymmetic neuroblast division.
JR|Bellen, Taylor, 2001
PG|147
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144479	AU 1 Bashaw et al.	YR 1 2001	TP 1 Abstract	TI 1 A novel Dbl family Rho GEF promotes axon attraction to the CNS midline and overcomes Robo repulsion.	REFM 1 Bellen, Taylor, 2001: 205		
ID|FBrf0144479
TP|abstract
|Drosophila meeting abstract
MABST|The key role of the Rho family GTPases -Rac, Rho and CDC42 -in regulating
| the actin cytoskeleton is well established. Increasing evidence suggests
| that the Rho GTPases and their upstream positive regulators-guanine
| nucleotide exchange factors (GEFs)-also play important roles in the control
| of growth cone guidance in the developing nervous system. Here we present
| the identification and molecular characterization of a novel Dbl family Rho
| GEF, GEF64C, that promotes axon attraction to the CNS midline in the
| embryonic Drosophila nervous system. GEF64C was identified in a gain of
| function interaction screen for enhancers of the Robo-DCC chimeric receptor
| phenotype. In sensitized genetic backgrounds, loss of GEF64C function
| causes a phenotype where too few axons cross the midline. In contrast,
| ectopic expression of GEF64C throughout the nervous system results in a
| phenotype in which far too many axons cross the midline, a phenotype
| reminiscent of loss of function mutations in the Roundabout (Robo)
| repulsive guidance receptor. Genetic analysis indicates that GEF64C
| over-expression can in fact overcome Robo repulsion. Surprisingly, evidence
| from genetic, biochemical and cell culture experiments suggests that the
| promotion of axon attraction by GEF64C is dependent on the activation of
| Rho, but not Rac or Cdc42.
AU|Bashaw
|G.J.
AU|Hu
|H.
AU|Nobes
|K.
AU|Goodman
|C.S.
YR|2001
TI|A novel Dbl family Rho GEF promotes axon attraction to the CNS midline and overcomes Robo repulsion.
JR|Bellen, Taylor, 2001
PG|205
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144480	AU 1 Armstrong et al.	YR 1 2001	TP 1 Abstract	TI 1 Identification of genes involved in gravitaxic responses in Drosophila.	REFM 1 Bellen, Taylor, 2001: 171		
ID|FBrf0144480
TP|abstract
|Drosophila meeting abstract
MABST|Gravity is an all-pervasive force on earth and generation of effective
| behavior by all higher organisms is predicated on perception of gravity. In
| Drosophila, the sense organs, processing centers and molecular pathways
| involved in receiving and responding to gravitational stimuli are unknown.
| We have used a gravitaxic maze testing paradigm to identify Drosophila
| mutants with aberrant gravitaxic responses. These mazes require flies to
| make up/ down choices at eight points and thus to exit at nine possible
| positions. The selection is therefore for mutant lines with maze exit
| profiles that are significantly different from those of appropriate control
| populations. In total we have screened approximately 1000 lines from two
| mutant collections: i) viable EMS mutants from the Zuker collection (C.
| Zuker, UC. San Diego) and ii) P {GAL4} insert-derived mutants generated by
| Armstrong and Kaiser (Glasgow University). A subset of 350 lines from the P
| {GAL4} collection that show expression in the adult CNS were used for our
| studies. Over 50 mutant lines with aberrant gravitaxic behavior have been
| isolated from the two collections. Most of these lines are normal for other
| complex behavior such as flight and courtship. The transposon insertion
| point for all 25 of the P {GAL4} lines producing aberrant gravitaxis has
| been established. In several lines, the affected gene has proved to be a
| gene with a previously established role in neural signaling or modeling. At
| least seven insertions appear to affect novel genes however. One of these
| insertions, which produces strong negative gravitaxis, is located in the
| ADH genomic region. Previous population genetics work in Hirsch's lab led
| to isolation of positive and negative gravitaxic populations and identified
| the ADH region as containing a locus affecting gravitaxic behavior (J Comp
| Physiol 110 p252, 1996). We have established that Hirsch's strongly
| negative gravitaxic population (" high line") carries a single amino acid
| change in the gene affected by our P {GAL4} insertion. This alteration is
| not present in three control strains examined, nor in the "low line"
| generated by Hirsch. In honor of the 40th anniversary of the first manned
| space flight by Yuri Gagarin, we have named the affected gene yuri. In
| adult heads, GAL4 expression from the yuri insert is found exclusively in
| the antennae and a small region of the CNS. Further characterization of
| yuri and other genes from our screen will be presented.
AU|Armstrong
|J.D.
AU|Texada
|M.J.
AU|Beckingham
|K.M.
YR|2001
TI|Identification of genes involved in gravitaxic responses in Drosophila.
JR|Bellen, Taylor, 2001
PG|171
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144481	AU 1 Berke and Wu	YR 1 2001	TP 1 Abstract	TI 1 Regional calcium regulation within cultured Drosophila neurons: Effects of altered cAMP metabolism by the learning mutations dunce and rutabaga.	REFM 1 Bellen, Taylor, 2001: 21		
ID|FBrf0144481
TP|abstract
|Drosophila meeting abstract
MABST|The dunce (dnc) and rutabaga (rut) mutations of Drosophila affect a
| cAMP-dependent phosphodiesterase and a Ca 2+ /CaM-regulated adenylyl
| cyclase, respectively. These mutations cause deficiencies in several
| learning paradigms and alter synaptic transmission, growth cone motility,
| and action potential generation. The cellular phenotypes are either Ca 2+
| -dependent (neurotransmission and motility) or mediate a Ca 2+ rise (action
| potential generation). However, inter-relations among these defects have
| not been addressed. We have established conditions for fura-2 imaging of Ca
| 2+ dynamics in the 'giant' neuron culture system of Drosophila. Using high
| K + depolarization of isolated neurons, we observed a larger, faster, and
| more dynamic response from the growth cone than cell body. This Ca 2+
| increase depended on an influx through Ca 2+ channels and was suppressed by
| the Na + channel blocker TTX. Altered cAMP metabolism by the dnc and rut
| mutations reduced response amplitude in the growth cone, while prolonging
| the response within the soma. The enhanced spatial resolution of these
| larger cells allowed us to analyze Ca 2+ regulation within distinct domains
| of the growth cone. We found that wild-type growth cones with motile
| filopodia exhibited a larger response to high K + -depolarization in the
| periphery than central domain. This distinction was disrupted by the rut
| mutation. Furthermore, both dnc and rut suppressed the facilitation by a
| prior conditioning depolarization (a decrease in response amplitude and
| waveform complexity). This may be related to previously described defects
| in the short-term plasticity of neurotransmission using a twin-pulse
| paradigm at the larval neuromuscular junction. The spatial resolution
| offered by optical imaging of cultured neurons complements
| electrophysiological studies in Drosophila. The two approaches in
| combination will greatly enhance the neurogenetic study of Ca 2+ -dependent
| processes in neuronal development and physiology.
AU|Berke
|B.
AU|Wu
|C.F.
YR|2001
TI|Regional calcium regulation within cultured Drosophila neurons: Effects of altered cAMP metabolism by the learning mutations dunce and rutabaga.
JR|Bellen, Taylor, 2001
PG|21
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144482	AU 1 Bier and Reiter	YR 1 2001	TP 1 Abstract	TI 1 How best to use Drosophila as a tool for analyzing human diseases.	REFM 1 Bellen, Taylor, 2001: 170		
ID|FBrf0144482
TP|abstract
|Drosophila meeting abstract
MABST|We have conducted a systematic analysis of human disease gene homologues in
| Drosophila melanogaster with the goal of identifying cases where the
| powerful molecular genetic tools available in Drosophila could be best used
| to greatest advantage in analyzing the human disease condition. Based on
| our analysis, we have initiated experimental studies into several human
| disease genes in Drosophila including those causing primary congenital
| glaucoma (CYP1B1 = Drosophila cyp18), the gene causing Angelman syndrome,
| and two genes potentially involved in Alzheimer's disease (TSA and PAG,
| which encode proteins that bind Presenilin). The objective of our PCG
| studies is to identify potential candidate genes in Drosophila
| corresponding to a suppressor locus on the short arm of chromosome 8 that
| can suppress the effects of mutations in CYP1B1 in a sub-population of
| Saudis. We have generated a series of mutant alleles in the Drosophila
| cyp18 gene which result in fluid flow problems reminiscent of those
| involved in PCG and are screening for second site suppressors of these
| mutations. We will determine whether any of the suppressors loci we
| identify in Drosophila have human homologues mapping to the short arm of
| human chromosome 8. We will then collaborate with Dr. B. Bejjani to ask
| whether any of these genes may correspond to the suppressor locus he is has
| mapped to 8p. In the case of the Angelman syndrome gene, which encodes E3
| ligase protein that targets selected proteins for degradation, we will
| screen for suppressors of loss-of-function mutations in the Drosophila
| Angelman syndrome (das) gene that cause lethality or semi -lethality in
| Drosophila and then collaborate with Dr. A. Beaudette's group to determine
| whether human or murine counterparts of these proteins are present in
| elevated levels in a human Angelman patient sample or in an Angelman model
| mouse. Finally, in the case of the novel genes interacting with Psn, we wil
| l collaborate with Dr. C. Von Broekhoven to determine whether any human
| homologs of these genes are map to candidate Alzheimer loci. From
| experimental approaches of this kind, we hope to validate Drosophila as a
| powerful model system for answering important unresolved questions in human
| medical genetics.
AU|Bier
|E.
AU|Reiter
|L.
YR|2001
TI|How best to use Drosophila as a tool for analyzing human diseases.
JR|Bellen, Taylor, 2001
PG|170
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144483	AU 1 Bissonnette et al.	YR 1 2001	TP 1 Abstract	TI 1 Characterization of a new allele of the gene twins (tws430).	REFM 1 Bellen, Taylor, 2001: 121		
ID|FBrf0144483
TP|abstract
|Drosophila meeting abstract
MABST|We have identified a new allele of the gene twins, a gene coding for a 55kd
| regulatory subunit of the enzyme Protein Phosphatase 2A (PP2A). This
| mutation disrupts both peripheral (PNS) and central (CNS) nervous system
| development of the adult Drosophila melanogaster, with no affect on
| embryonic development. Within the CNS, neuroblasts in the thoracic ganglion
| and central brain fail to enter the cell cycle and produce no progeny,
| while optic lobe neuroblasts do divide producing progeny. PNS phenotypes
| include a loss of occipital hairs and a decrease in the number of
| dorsal-central and s cutellar hairs on the thorax. PP2A has been shown to
| play a role in PNS development of the post-embryonic fly. In the PNS, a
| sensory organ precursor (SOP) undergoes one symmetric division, which is
| followed by a single division of the progeny. The result is four cells that
| differentiate into the sensory hair and socket on the external side of the
| cuticle, and the neuron and sheath cell on the interior. PP2A is involved
| in specifying one of these fates to the four progeny. This new allele of
| twins shows a disrupted pattern of sensory hair distribution. We believe
| PP2A plays an additional role, acting earlier to help specify the field of
| cells that become SOP's. This new allele of twins will help better define
| the role of PP2A in post-embryonic development of the PNS and CNS.
AU|Bissonnette
|D.M.
AU|Ng
|D.M.
AU|Booker
|R.
YR|2001
TI|Characterization of a new allele of the gene twins (tws430).
JR|Bellen, Taylor, 2001
PG|121
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144484	AU 1 Blau et al.	YR 1 2001	TP 1 Abstract	TI 1 The role of VRILLE and PDP1 in circadian rhythms.	REFM 1 Bellen, Taylor, 2001: 95		
ID|FBrf0144484
TP|abstract
|Drosophila meeting abstract
MABST|Clock genes form a negative feedback loop that regulates cycling expression
| of their own genes in pacemaker cells. These pacemaker cells presumably
| then release signals at different times of day that tell the fly when to be
| active and when to sleep. We previously identified a transcription factor
| called vrille on the basis of its rhythmic clock-dependent expression.
| Cycles of vrille RNA and protein are required for a functional clock since
| over-expression of vrille causes molecular and behavioral arrhythmicity.
| How does VRILLE feed back to the clock? Our results indicate that VRILLE
| directly regulates cycling of the dClock gene, whose RNA and protein levels
| also oscillate in a clock-dependent manner. VRILLE is likely to act as a
| transcriptional repressor of dClock expression. What then activates dClock
| expression? We searched for VRILLE-related genes and found Par Domain
| Protein 1 (Pdp1), a gene which encodes a transcription factor with an
| almost identical DNA-binding domain to VRILLE, and whose expression is also
| clock-dependent. Over-expression of wild type Pdp1 causes arrhythmicity, as
| does over-expression of a dominant-negative form of Pdp1 ñ indicating that
| Pdp1 is a likely new clock gene. We are testing the hypothesis that VRILLE
| and PDP1 proteins have opposite effects on the dClock promoter, and are
| responsible for regulating cycles of dClock expression.
AU|Blau
|J.
AU|Cyran
|S.
AU|Buschsbaum
|A.
AU|Lin
|M.
AU|Reddy
|K.
AU|Storti
|B.
YR|2001
TI|The role of VRILLE and PDP1 in circadian rhythms.
JR|Bellen, Taylor, 2001
PG|95
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144485	AU 1 Block et al.	YR 1 2001	TP 1 Abstract	TI 1 Clonal analysis of embryonic and post-embryonic neurogenesis in the ventral nerve cord.	REFM 1 Bellen, Taylor, 2001: 181		
ID|FBrf0144485
TP|abstract
|Drosophila meeting abstract
MABST|The generation of the central nervous system in Drosophila occurs in two
| waves, with more than 90% of the adult CNS being produced
| post-embryonically. Despite its clear importance, little is known regarding
| postembryonic neurogenesis in the ventral nerve cord. This is largely due
| to technical difficulties, which until recently have prevented the study of
| neuroblasts (NBs) past their earliest divisions. We have used the MARCM
| technique to analyse both embryonic and post-embryonic neurogenesis in the
| ventral nerve cord. This has enabled NB lineages to be determined, from
| first division to last. By creating clones at different time points during
| development, we are able to examine progressive changes in the neuron types
| produced by a single NB and determine whether there are significant
| transitions between embryonic and post -embryonic clones. Significantly,
| motorneurons have been found to be produced post -embryonically in thoracic
| and terminal segments, which are specialised for adult specific behaviours,
| but have not so far been observed in abdominal segments. The ongoing
| analysis will enable key questions regarding neurogenesis and the
| functional organisation of the adult ventral nerve cord to be addressed.
| For example, do clonally related neurons innervate common regions of
| neuropile or share common functional roles? Is there a relationship between
| NB position and the central organisation of its progeny? Do the properties
| of neurons in a clone change as the lineage progresses? Are all NBs
| multipotent? Is the somatotopic and modality specific organisation of
| sensory afferents mirrored in the organisation of the central nervous
| system? Is there a corresponding anatomical segregation of interneurons?
| Preliminary results will be presented.
AU|Block
|L.
AU|Williams
|D.
AU|Shephard
|D.
YR|2001
TI|Clonal analysis of embryonic and post-embryonic neurogenesis in the ventral nerve cord.
JR|Bellen, Taylor, 2001
PG|181
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144486	AU 1 Botella et al.	YR 1 2001	TP 1 Abstract	TI 1 Identification of novel genes and mechanisms of neurodegeneration in Drosophila.	REFM 1 Bellen, Taylor, 2001: 165		
ID|FBrf0144486
TP|abstract
|Drosophila meeting abstract
MABST|In the last years Drosophila melanogaster has been proved useful for the
| study of basic mechanisms of neurodegeneration. While some groups have used
| it successfully to model some known neurodegenerative diseases, we have
| tried to identify and study novel genes involved in mechanisms of
| age-related neurodegenerative disorders. Several histological screens have
| been performed to isolate mutants that show brain degeneration. Here we
| present two cases of our best studied mutants in which neuronal
| degeneration occurs via different mechanisms: Total and partial
| loss-of-function mutation in the Drosophila gene RasGAP (vap), a negative
| regulator of the Egfr/ Ras pathway, lead to age-related neuronal
| degeneration with a morphology resembling that of cell death type 2
| (autophagy). We show that mutations in RasGAP cause an aberrant regulation
| of RAS that leads to a deregulated activation of the MAPK transduction
| cascade. Thus our results on the vap mutant provide new insights into the
| role of this signal transduction cascade in the maintenance of the
| Drosophila adult nervous system and a useful model to study autophagy in
| the context of neuronal cell death. >From the same screen we have also
| isolated sniffer, a member of the short-chain dehydrogenases/ reductases
| family. In sniffer mutants the phenotype is especially evident in the
| cortex of the first optic ganglion, the lamina, where neurons die in an
| age-dependent manner followed by apoptosis of glial cells. Mutant flies
| show, besides brain degeneration, a locomotor phenotype and reduced life
| span. We show that the function of sniffer is required to prevent neuronal
| apoptosis induced by oxidative stress. Further characterization of this
| mutant together with experiments to elucidate the function of this enzyme
| will be presented. The analysis of sniffer provides an important model to
| get insights into the causal mechanisms of oxidative stress in the process
| of neurodegeneration and life span.
AU|Botella
|J.A.
AU|Kretzschmar
|D.
AU|Kiermayer
|C.
AU|Hughes
|D.
AU|Becker
|K.
AU|Schneuwly
|S.
YR|2001
TI|Identification of novel genes and mechanisms of neurodegeneration in Drosophila.
JR|Bellen, Taylor, 2001
PG|165
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144487	AU 1 Boyle and Thomas	YR 1 2001	TP 1 Abstract	TI 1 Analysis of the role of Eph RTK, dek in axon pathfinding and target recognition in the embryonic CNS.	REFM 1 Bellen, Taylor, 2001: 206		
ID|FBrf0144487
TP|abstract
|Drosophila meeting abstract
MABST|Studies of the large family of vertebrate Eph receptor tyrosine kinases and
| their ligands, the Ephrins, have implicated a role for this gene family in
| axon guidance. In Drosophila, there is a single Eph family member, named
| DEK, which exhibits equal similarities to both the EphA and EphB subclasses
| of receptors. Consistent with a possible role in axon guidance, DEK is
| restricted to the embryonic CNS at a time when neurons are extending axons
| and is targeted to axons and growth cones. A search of the Drosophila
| genome database uncovers a single EPHRIN that contains regions of homology
| to both vertebrat e type A and type B ligands. Curiously, we have found by
| in situ hybridization that ephrin, like dek, is expressed throughout the
| embryonic CNS. To determine their roles in nervous system development, we
| have used a P element mobilization scheme to generate mutations in dek and
| ephrin. Both genes map within 42 Kb of one another on the 4th chromosome.
| We mobilized a lethal P element located 155 Kb away from dek and selected
| those insertions that both reverted the lethality (thus indicating a
| mobilization event) and mapped by linkage to the 4th chromosome. Insertion
| sites for each of the lines generated were determined by sequencing
| fragments generated by inverse PCR. From the 55 lines generated, we
| recovered an insertion, P114, that maps 3 kb upstream of t he dek
| transcriptional start site. P114 is currently being used to generate
| excisions deleting the dek coding sequences. The consequence of loss of dek
| function on neuronal development will be presented.
AU|Boyle
|M.
AU|Thomas
|J.
YR|2001
TI|Analysis of the role of Eph RTK, dek in axon pathfinding and target recognition in the embryonic CNS.
JR|Bellen, Taylor, 2001
PG|206
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144488	AU 1 Phelps et al.	YR 1 2001	TP 1 Abstract	TI 1 Asymmetric cell division in the embryonic CNS.	REFM 1 Bellen, Taylor, 2001: 9		
ID|FBrf0144488
TP|abstract
|Drosophila meeting abstract
MABST|One way to generate diversity is to ensure that when a cell divides each of
| its daughters assumes a distinct identity. This can be simply achieved by
| segregating a cell fate determinant to only one of the two daughter cells
| at cell division. Prior to neuroblast cell division, Prospero and its mRNA
| are localised to the basal cortex and are partit ioned to the GMC at
| cytokinesis. Prospero is then released and enters the nucleus where it
| regulates genes that direct GMC fate. We are investigating the molecular
| mechanisms that direct the asymmetric segregation of cell fate determinants
| and their mRNAs. The coiled-coil domain protein, Miranda, is essential for
| the segregation of both Prospero protein and its mRNA. Miranda binds
| directly to Prospero and to Staufen, which in turn binds Prospero mRNA.
| Studies in which the actin cytoskeleton is disrupted demonstrate that
| F-actin is essential for localisation of Miranda. The dynamics of
| asymmetric localisation and the dependence on F-actin suggest a role for
| myosin motor proteins in asymmetric cell division. We have shown that
| cytoplasmic myosin II plays an integral role in localising determinants in
| neuroblasts. Myosin II is itself localised asymmetrically in neuroblasts,
| and appears to preclude binding of determinants to the apical cortex.
| Myosin II is the homologue of C. elegans NMY-2, which is required to
| localise PAR proteins in the one-cell embryo (Guo and Kemphues, 1996),
| revealing a conserved role for myosin II motors in mediating
| actin-dependent asymmetric segregation. In Drosophila, myosin II has been
| shown to interact directly with the tumour suppressor Lethal giant larvae,
| which is also required for asymmetric cell division (Ohshiro et al., 2000;
| Peng et al., 2000). We are using time lapse confocal microscopy to follow
| cell fate determinants and cytoskeletal proteins simultaneously in living
| embryos. For theses experiments, we have fused different spectral variants
| of GFP to Miranda, Prospero, Staufen and Myosin, actin and microtubules.
AU|Phelps
|C.B.
AU|Barros
|C.
AU|Brand
|A.H.
YR|2001
TI|Asymmetric cell division in the embryonic CNS.
JR|Bellen, Taylor, 2001
PG|9
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144489	AU 1 Brody et al.	YR 1 2001	TP 1 Abstract	TI 1 A cDNA screen for genes that are dynamically expressed during the generation of embryonic neural lineages.	REFM 1 Bellen, Taylor, 2001: 64		
ID|FBrf0144489
TP|abstract
|Drosophila meeting abstract
MABST|During neuroblast (NB) lineage development, temporally ordered transitions
| in NB gene expression have been shown to accompany the changing repertoire
| of functionally diverse cells generated by NBs. For example, we have
| described a transcription factor network, the Hb-> Pdm-> Cas-> Gh
| cascade 1,2 , that regulates temporal transitions in gene expression during
| CNS lineage development. In order to discover additional components of this
| network, both upstream and downstream, we have carried out an expression
| screen. A cDNA library was prepared from 2,600 individually dissected 8.5h
| (stage 11) embryonic heads. The unamplified library was screened to remove
| widely expressed sequences. cDNAs corresponding to 4,500 temporally
| regulated genes have been partially sequenced to determine the
| corresponding genes. We have subsequently carried out over 2,000 in situ
| hybridizations in order to discover which of these genes are expressed in
| neural precursors. Our expression studies have revealed 57 new or partially
| characterized genes that are dynamically expressed during CNS development.
| The expression patterns of these CNS lineage markers will be presented.
| Most of these genes have been predicted by the Drosophila genome project, a
| few have already been cloned, but some are undefined, that is they were not
| among the genes predicted by the Drosophila genome project. In addition, we
| provide information on 823 known and 1,621 previously uncharacterized genes
| whose corresponding cDNAs have been identified in the screen. Information
| about all of these genes is available at the web site entitled "BrainGenes:
| a search for Drosophila neural precursor genes": http:// sdb. bio. purdue.
| edu/ fly/ brain/ ahome. htm. We will describe addit-ional experiments
| designed to reveal the temporal regulation of these and other CNS
| determinates. 1. Kamgadur, et al. Genes & Development 12: 246-260
| (1998) 2. Brody and Odenwald, Developmental Biology, 226: 34-44 (2000)
AU|Brody
|T.
AU|Stivers
|C.
AU|Nagel
|J.
AU|Odenwald
|W.F.
YR|2001
TI|A cDNA screen for genes that are dynamically expressed during the generation of embryonic neural lineages.
JR|Bellen, Taylor, 2001
PG|64
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144490	AU 1 Broihier and Skeath	YR 1 2001	TP 1 Abstract	TI 1 Homeodomain protein extra-extra: The Drosophila Hb9 homolog, directs neuronal fate via cross-repressive and cell non-autonomous mechanisms.	REFM 1 Bellen, Taylor, 2001: 10		
ID|FBrf0144490
TP|abstract
|Drosophila meeting abstract
MABST|To initiate a systematic analysis of the genetic basis of neuronal fate
| determination, we undertook a saturation mutagenesis to identify genes that
| regulate the development of a specific set of CNS neurons. Here we present
| the identification and characterization of one mutant isolated in this
| screen, extra-extra (exex). exex is the sole Drosophila homolog of the
| closely-related vertebrate genes Hb9/ MNR2, which encode homeodomain
| factors required for motorneuron (MN) development. We identified exex via
| its ability to repress Even-skipped (Eve), a homeodomain protein expressed
| in all dorsally-projecting MNs in the Drosophila embryonic CNS. We find
| that Exex is expressed in ventrally-projecting MNs and is required for
| their differentiation. Furthermore, we demonstrate that Exex and Eve are
| expressed in mutually-exclusive patterns and repress each other to
| distinguish ventrally and dorsally-projecting MNs. Lastly, we show that
| exex is required to repress the LIM homeodomain protein Lim3 in a subset of
| dorsally-projecting MNs. As these MNs express Eve, and not Exex, Exex acts
| cell non-autonomously to restrict lim3 expression.
AU|Broihier
|H.T.
AU|Skeath
|J.B.
YR|2001
TI|Homeodomain protein extra-extra: The Drosophila Hb9 homolog, directs neuronal fate via cross-repressive and cell non-autonomous mechanisms.
JR|Bellen, Taylor, 2001
PG|10
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144491	AU 1 Bronk et al.	YR 1 2001	TP 1 Abstract	TI 1 Different domains mediate different functions of Drosophila cysteine-strong protein at nerve terminals.	REFM 1 Bellen, Taylor, 2001: 22		
ID|FBrf0144491
TP|abstract
|Drosophila meeting abstract
MABST|Multiple steps, vesicle fusion, Ca 2+ entry, and Ca 2+ clearance, might be
| regulated by the synaptic vesicle-associated cysteine-string protein (CSP).
| Null mutations in Drosophila csp increase stimulus -evoked presynaptic Ca
| 2+ levels but reduce evoked release at larval neuromuscular junctions. 1
| Therefore, we hypothesize that CSP increases release by promoting a
| downstream step of Ca 2+ -triggered fusion, and maintains appropriate Ca 2+
| levels by regulating Ca 2+ entry and/ or clearance. To better understand
| CSP's action, we initiated a systematic in vivo structure/ function study.
| Specifically, we analyzed the effects of expressing mutant CSP's lacking
| the following conserved domains at csp null terminals: (1) the J-domain
| mediating the CSP-Hsc70 interaction and (2) the "linker domain" (L-domain)
| whose protein interactions are unknown. Expression of ?J-CSP restored
| normal levels of evoked neurotransmitter release in csp nulls at 23 o C,
| but did not restore viability. ?J-CSP expression also did not revert the
| elevated resting Ca 2+ levels at 34 o C, which are characteristic of csp
| null mutants. Interestingly, ?J-CSP expression caused a 4-fold increase in
| spontaneous mEJP frequency at 32 o C, while csp null mutants showed a
| normal frequency. This "additional" defect is consistent with the idea that
| ?J-CSP expression restores Ca 2+ triggered fusion in csp nulls, but not the
| intraterminal resting Ca 2+ levels at elevated temperatures. In contrast to
| ?J-CSP, ?L-CSP expression restored normal transmission at 23 o C and normal
| resting Ca 2+ levels at 34 o C but not viability. In addition,
| intraterminal Ca 2+ levels were still increased upon nerve stimulation. Our
| current results show that different domains of CSP mediate different
| functions at nerve terminals. Surprisingly, the J -domain is not essential
| for Ca 2+ triggered fusion but rather for Ca 2+ entry/ extrusion. Ca 2+
| entry/ extrusion is affected differently by ?J-CSP and ?L-CSP, but it
| remains to be seen whether this difference is due to a change in the rate
| of Ca 2+ entry, Ca 2+ clearance, and /or to a different "set point" for the
| regulation of Ca 2+ homeostasis. Future work will resolve whether these
| domains mediate the known interactions of CSP with Ca 2+ channels,
| G-proteins, and syntaxin.
AU|Bronk
|P.
AU|Dawson-Scully
|K.D.
AU|Nie
|Z.
AU|Atwood
|H.L.
AU|Zinsmaier
|K.E.
YR|2001
TI|Different domains mediate different functions of Drosophila cysteine-strong protein at nerve terminals.
JR|Bellen, Taylor, 2001
PG|22
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144492	AU 1 Burnette and Hirsh	YR 1 2001	TP 1 Abstract	TI 1 Identification of neurons modulating responses to crack cocaine in Drosophila.	REFM 1 Bellen, Taylor, 2001: 96		
ID|FBrf0144492
TP|abstract
|Drosophila meeting abstract
MABST|We are using Drosophila as a model to identify novel genetic pathways
| involved in modulating responses to crack cocaine. Wild type flies
| repeatedly exposed to the same dose of cocaine show enhanced responses, a
| process known as sensitization. Previous results have shown that the
| circadian gene products period, clock, and cycle fail to sensitize and thus
| are required for sensitization, whereas timeless has no role in the process
| (Andretic et al. Science (1999) 285( 5430): 1066-8285). This suggests that
| there is a subset of period expressing cells involved in cocaine response
| modulation but is outside of the clock. To further differentiate between
| the clock mechanism and cocaine responses we are examining cocaine
| responses subsequent to transiently blocking synaptic transmission using
| the UAS-shi ts1 system. We have driven the expression of UAS-shi ts1 with a
| GAL4 driver that expresses in most dopa decarboxlyase expressing cells.
| When raised and tested at the permissive temperature, these flies show
| normal locomotor responses to the initial dose of cocaine. Flies raised at
| the permissive temperature but tested at 24? C show greatly reduced
| responses to cocaine. This result is consistent with findings in mammals
| and flies that transiently blocking dopamine signaling reduces locomotor
| responses to cocaine. Flies raised and tested at 24? C are hypersensitive
| to cocaine, which suggests that developmental compensation has taken place,
| as observed previously when tetanus toxin expression was driven with
| Ddc-GAL4 drivers (Li et al (2000). Curr. Biol. 10( 4): 211-4). Flies
| hemizygous for per-GAL4 and UAS-shi ts1 insertions are hypersensitive to
| cocaine and surprisingly, become resistant upon repeated exposures when
| grown and tested at 24? C. This differs from the per 01 , which remains
| equally responsive after repeated exposures. We will conduct an enhancer
| trap screen to identify specific neurons involved in modulating cocaine
| responses. We will also determine whether neurons of the central circadian
| oscillator are required for the modulation of cocaine responses using the
| pdf-GAL4 and other available GAL4 insertion lines.
AU|Burnette
|J.
AU|Hirsh
|J.
YR|2001
TI|Identification of neurons modulating responses to crack cocaine in Drosophila.
JR|Bellen, Taylor, 2001
PG|96
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144493	AU 1 Cai et al.	YR 1 2001	TP 1 Abstract	TI 1 D-Homer function is required for telophase rescue in Drosophila embryonic neuroblast divisions.	REFM 1 Bellen, Taylor, 2001: 148		
ID|FBrf0144493
TP|abstract
|Drosophila meeting abstract
MABST|Asymmetric divisions of neural ste m cells, neuroblasts (NBs) produce
| diverse neural cell types required for the central nervous system
| formation. It has been suggested that two asymmetry-controlling mechanisms,
| Insc -dependent and Insc-independent, are involved in NB division. During
| NB divisions, a group of apically localized proteins, such as Bazooka
| (Baz), Inscuteable (Insc) and Partner of Inscuteable (Pins) forms an apical
| complex and controls various downstream events of asymmetric divisions. In
| the mutants that apical complex is defective, the basal localization of
| cell fate determinants in dividing NBs is affected during early phases of
| mitosis. However, late in mitosis the cell fate determinants are
| redistributed to and enriched in the basal/ lateral cortex of mutant NBs
| from where the future ganglion mother cells (GMCs) will "bud" off. This
| Insc-independent phenomenon has been referred to as "telophase rescue". The
| mechanism of "telophase rescue" is not clear at present. We have cloned the
| d-homer, the Drososphila homolog of homer gene in mammals. D-Homer contains
| a conserved amino-terminal EVH-1 domain and a carboxyl-terminal motif with
| a predicted coiled-coil (CC) structure. During early neurogenesis the
| sub-cellular localization of D-Homer in dividing NBs is cell cycle
| regulated. In interphase neuroblasts, D-Homer is distributed evenly
| throughout cell cortex. However, once NBs enter mitosis, localization of
| D-Homer becomes asymmetric. D-Homer is enriched to the apical cortex of
| mitotic NBs in prophase. In metaphase, D-Homer forms an apical crescent and
| remains apical throughout the rest of mitosis. The asymmetric D-Home
| localization is Insc-independent. Two viable deletion lines were recovered
| from the imprecise excision of the EP-element insertion line and both
| deletions are antigen-minus as judged by antibody staining, suggesting that
| D-Homer is not essential for animal viability. Homozygous d-homer does not
| show any obvious phenotypes in asymmetric NB divisions. However, when
| d-Homer is removed in insc mutant, basal proteins, such as Mir/ Pro and
| Pon/ Numb, are evenly distributed to the cortex of the dividing NBs and the
| redistribution of basal proteins to the future GMC budding site (telophase
| rescue) does not occur. This observation suggests that d-Homer could be the
| first identified member of the Insc-independent mechanism that is
| responsible for the "telophase rescue".
AU|Cai
|Y.
AU|Yu
|F.
AU|Chia
|W.
AU|Yang
|X.
YR|2001
TI|D-Homer function is required for telophase rescue in Drosophila embryonic neuroblast divisions.
JR|Bellen, Taylor, 2001
PG|148
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144494	AU 1 Adachi et al.	YR 1 2001	TP 1 Abstract	TI 1 Expression of eyeless in the Drosophila brain depends on a complex of enhancers.	REFM 1 Bellen, Taylor, 2001: 182		
ID|FBrf0144494
TP|abstract
|Drosophila meeting abstract
MABST|The Drosophila Pax-6 homolog eyeless plays an important role in the
| development of several brain neuropils including the mushroom bodies,
| central complex, and optic lobes. Analysis of Eyeless distribution in
| embryonic, larval, pupal, and adult brains suggests that the expression of
| eyeless in the various neuropils is governed by separable,
| neuropil-specific enhancer elements. To start to address how complex brains
| are generated by the region-specific expression of transcription factors,
| and of their transcriptional target genes, we pursued the transcriptional
| regulation of eyeless. We have characterized the GAL4 enhancer trap line
| OK107 as an insertion in the eyeless upstream region that reproduces many
| critical features of the eyeless expression pattern in the brain. To
| further identify individual, neuropil -specific regulatory sequences, a
| detailed analysis of the upstream region and the first and second intron of
| the eyeless gene was performed using in vivo reporter gene analysis. We
| have identified DNA elements of the eyeless gene that generate preferential
| expression in the central brain, and the mushroom bodies in particular, and
| the optic lobes. A detailed analysis of the mushroom body expression
| pattern with various markers reveals that expressio n in the different
| neuropils appears to depend on several physically distinct regulatory
| sequences that interact to generate the final pattern. Sequence analysis of
| the regulatory elements has identified candidate upstream factors that are
| being tested. This study will be very valuable not only to understand the
| transcriptional circuitry that generates complex brain centers, but also to
| generate tools for molecular and genetic interference with integrated
| neural processes such as vision, or learning and memory.
AU|Adachi
|Y.
AU|Clements
|J.
AU|Hauck
|B.
AU|Kang
|Y.Y.
AU|Kawauchi
|H.
AU|Walldorf
|U.
AU|Furukubo-Tokunaga
|K.
AU|Callaerts
|P.
YR|2001
TI|Expression of eyeless in the Drosophila brain depends on a complex of enhancers.
JR|Bellen, Taylor, 2001
PG|182
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144495	AU 1 Carlo et al.	YR 1 2001	TP 1 Abstract	TI 1 Molecular analysis of the fruitless stimulation factor LOCUS.	REFM 1 Bellen, Taylor, 2001: 97		
ID|FBrf0144495
TP|abstract
|Drosophila meeting abstract
MABST|The original fruitless mutant was obtained from an X-ray mutagenesis screen
| as a male sterile. This fru 1 mutant contains a short inversion: In( 3R)
| 90C; 91B. The distal breakpoint is now called fru 1 , in that other
| fru-mutant alleles are located in 91B. At least three distinct phenotypes
| are caused by homozygousity for both breakpoints in the fru 1 inversion.
| First, males are behaviorally sterile; they do not curl their abdomens in
| attempts to copulate. Second, they form male-exclusive courtship chains.
| Third homozygotes and to a degree fru 1 /+ heterozygotes elicit courtship
| from normal males. The first two phenotypes were mapped to the lesion in
| 91B. The latter phenotype has been attributed to the 90C region; this
| putative genetic locus has been named fruitless stimulation factor ( fsf)
| and is the subject of the studies reported here. . Analysis of fsf has the
| potential to provide useful information about courtship stimuli, because.
| hemizygosity for the breakpoint at this locus in males caused them to be
| courted by other males. A mature wild-type male is barely courted,
| suggesting that the fsf locus controls a factor involved in establishing
| the non-stimulating features of normal maleness. We suggest further that
| understanding the gene whose existence is implied by the fsf breakpoint
| will provide specific insights into pheromonal courtship stimuli, given
| that paralyzed fsf/ 90C-deletion males elicit extremely high levels of
| courtship, whereas immobilized wild-type males are almost completely
| ignored. Using ligation-mediated PCR; we have cloned both the distal and
| proximal ends of the fru 1 inversion and have mapped the breakpoints down
| to the nucleotide level. The centromere-distal end of the inversion in 91b
| maps about 3 kb upstream of a proposed fru transcription start site within
| that (91B) locus (the so-called P1 such site, located ca. 130 kb upstream
| of the fru ORF). The proximal end of the inversion has been located within
| the Celera genomic sequence. This 90C breakpoint occurred between two
| transcribed regions. The expressed sequence proximal to the breakpoint has
| strong homology to a mammalian gene called Rab-interacting-molecule (Rim).
| RIM protein has been demonstrated to be regulator of RAB3 in mammals; the
| latter is involved the fusion of vesicles to the cell membrane. RIM is
| represented by several non-identical EST's in the Drosophila database.
| Northern analysis has demonstrated that numerous transcripts can be
| detected with a probe to a common region of Drosophila RIM, mRNA
| heterogeneity that is likely to arise from multiple promoters and
| alternative splicing. RIM is a good candidate for being the gene
| responsible for the fsf phenotype. The second expressed sequence, located
| distal to the breakpoint, is the previously characterized couch potato
| (cpo) gene, which encodes a widely expressed RNA-binding protein associated
| (in viable hypomorphic cpo mutants) with general sluggishness. To help
| determine which of these two transcription units is associated with the fsf
| phenotype, a P-element located within the cpo transcription unit was
| excised. Of the 54 lines obtained that were homozygous viable and no longer
| express the transposon marker, 15 produced males that were sterile when
| homozygous for the newly derived 3rd chromosome. Homozygous females from
| all such lines were fertile. Therefore, cpo may play a role in male
| fertility, a phenotype in the same ballpark as establishment normal male
| (fsf + ) pheromones. These excision lines are being tested to determine
| whether homozygous males can elicit courtship from wild type males and to
| assess the cause of the male sterility (e. g., pre-mating behavioral
| deficits vs. defective sperm). Molecularly these lines are being
| characterized to determine which genes were effected by the P-element excisions.
AU|Carlo
|T.
AU|Villella
|A.
AU|Hall
|J.C.
YR|2001
TI|Molecular analysis of the fruitless stimulation factor LOCUS.
JR|Bellen, Taylor, 2001
PG|97
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144496	AU 1 Carney and Taylor	YR 1 2001	TP 1 Abstract	TI 1 A putative vesicle cargo receptor protein is required for female oviposition behavior.	REFM 1 Bellen, Taylor, 2001: 176		
ID|FBrf0144496
TP|abstract
|Drosophila meeting abstract
MABST|Little is known about how sex-specific nervous systems are created and
| produce a desired behavioral outcome. We have approached this problem in
| the Drosophila female by screening for genes involved in female-specific
| mating or oviposition behaviors, with the hope of identifying genetic
| cascades functioning in sex-specific neuronal differentiation and signal
| transmission. Mutations in a newly identified gene result in the loss of
| oviposition behavior and the retention of phenotypically normal eggs in the
| oviducts of mated mutant females. Sequence analysis reveals that this gene
| has homology to a family of vesicle cargo receptor proteins found in
| numerous taxa. It is expressed in both adult females and males, potentially
| in a sex-specific manner. Two independent P element insertion alleles
| abolish all identified transcripts but produce an obvious phenotype only in
| females. Enhancer trap analysis of adult females from each P line reveals
| expression in the central nervous system but not other tissues. However, in
| situ analysis of sectioned adult females indicates that transcripts
| predominantly localize to ovarian follicle cells. Currently, only two other
| genes are known whose mutant phenotypes include egg retention.
| dissatisfaction (dsf )is an output gene of the sex determination hierarchy
| that is needed for receptivity to mating as well as oviposition behavior.
| Tyramine Beta-Hydroxylase (TBH) is needed for production of the
| neurotransmitter octopamine, which functions in egg-laying behavior.
| Genetic and molecular data suggest that the putative cargo receptor
| functions outside of either of these two pathways and may be a component of
| another, parallel signaling pathway needed for oviposition.
AU|Carney
|G.E.
AU|Taylor
|B.J.
YR|2001
TI|A putative vesicle cargo receptor protein is required for female oviposition behavior.
JR|Bellen, Taylor, 2001
PG|176
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144497	AU 1 Leaman and Carthew	YR 1 2001	TP 1 Abstract	TI 1 The function and dysfunction of CDK5 in neuronal development and degeneration.	REFM 1 Bellen, Taylor, 2001: 166		
ID|FBrf0144497
TP|abstract
|Drosophila meeting abstract
MABST|One of the neuropathological hallmarks of Alzheimers Disease (AD) is the
| presence of neurofibrillary tangles (NFT) that are composed of aggregates
| of the protein Tau in abnormal conformations and phosphorylation states.
| The mammalian kinase CDK5 phosphorylates Tau in vitro and is thought to
| play a role in Tau's transition into NFTs. Here we explore the role of
| Drosophila CDK5 and its activator protein Dp35 in neuronal development and
| degeneration. We find that CDK5 and Dp35 are required in embryonic CNS
| neurons for growth cone guidance and motility. We also find axon branching
| is normally suppressed by the action of CDK5. We present genetic evidence
| that places CDK5 activation downstream of growth cone guidance cues
| received by neurons of the CNS. Tissue from AD brains contains a
| proteolyzed form of human p35 in which its myristoylation signal is cleaved
| off, resulting in abnormal cellular distribution of the smaller p25. We
| expressed a truncated form of Dp35 in Drosophila neurons that structurally
| mimics the AD p25 fragment. Dp25 expression during development resulted in
| impaired development of the adult CNS projection systems and a block in
| eclosion behavior. In contrast Dp35 expression had no effect nor did Dp25
| expression in non-neuronal tissues. The Dp25 gain-of-function phenotype was
| suppressed by reducing the dosage of the cdk5 gene, suggesting that CDK5 is
| necessary for the neuronal dysfunction. Dp25 expression after adult
| eclosion resulted in reduced lifespan and neuronal apoptosis. In animals
| that co-expressed human Tau protein, these effects were accompanied by
| hyperphosphorylation of human Tau and its conformational change to a
| pre-NFT state. Co-expression of human Tau and full-length Dp35 had no
| adverse affect on Tau or neuronal viability. These data strongly support a
| causative relationship between structural changes in p35 and Tau that
| precede neuronal degeneration.
AU|Leaman
|D.
AU|Carthew
|R.
YR|2001
TI|The function and dysfunction of CDK5 in neuronal development and degeneration.
JR|Bellen, Taylor, 2001
PG|166
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144498	AU 1 Castro et al.	YR 1 2001	TP 1 Abstract	TI 1 Repression by Su(H) in Notch-mediated lateral inhibition.	REFM 1 Bellen, Taylor, 2001: 122		
ID|FBrf0144498
TP|abstract
|Drosophila meeting abstract
MABST|Notch (N) signaling plays a critical role in a wide variety of cell fate
| decisions during development. It is used to specify distinct cell fates
| among interacting cells and occurs in three general settings: 1) between
| rows of juxtaposed cells in which each row adopts a distinct fate; 2)
| binary cell fate decisions between sister cells in asymmetric cell
| divisions; and 3) cell fate decisions wherein a single cell uses N
| signaling to laterally inhibit surrounding cells from adopting its fate.
| The canonical N pathway involves two interacting cells: Delta ligand on the
| non-responding cell binds N receptor on the responding cell, inducing
| proteolytic cleavage and nuclear translocation of the N intracellular
| domain, which then complexes with the ubiquitously expressed transcription
| factor Suppressor of Hairless [Su( H)] to activate N target genes. While
| earlier models depicted Su( H) as having a strictly activating role in N
| responder cells, recent evidence has shown that Su( H) has an additional
| and critical repressive role in non-responders, serving to repress N target
| genes in the se cells. This repressive function of Su( H) has been shown in
| N signaling between rows of cells (Morel et al.) and during binary cell
| fate decisions (our lab; Barolo et al.). Recently, we have been able to
| demonstrate that this novel repression function also plays a role in
| lateral inhibition, the third setting of N signaling. During imaginal disc
| development, clusters of cells (proneural clusters, PNC) defined by their
| expression of proneural proteins (PN) are formed. One cell is selected to
| become a committed N non-responder, signaling the responding cluster cells
| to express N target genes (such as those of the Enhancer of split [E( spl)]
| Complex) which repress PN levels in these cells. PNs therefore accumulate
| to high levels in the non-responder and confer on it the sensory organ
| precursor (SOP) fate. The SOP then divides to give rise to a mechanosensory
| bristle. Using an enhancer-reporter construct, derived from the E( spl) ma
| gene, that expresses strictly in non-SOP (responder) cells of PNCs, we have
| found by mutational analysis that Su( H) binding sites are critical not
| only for gene activation in the non-SOP cells but also for repression in
| SOPs. Loss of this repression results in ectopic expression of the reporter
| in SOPs. This ectopic expression is furthermore directly dependent on the
| integrity of PN protein binding sites. We are currently investigating the
| nature of the repressive complex, the importance of this repression for
| preserving the SOP fate, and the ability to confer Su( H)-mediated
| repression on a heterologous enhancer that is normally active strictly in SOPs.
AU|Castro
|B.
AU|Barolo
|S.
AU|Posakony
|J.W.
YR|2001
TI|Repression by Su(H) in Notch-mediated lateral inhibition.
JR|Bellen, Taylor, 2001
PG|122
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144499	AU 1 Certel et al.	YR 1 2001	TP 1 Abstract	TI 1 Regulation of motor axon targeting by the combinatorial activity of POU and LIM homeodomain proteins.	REFM 1 Bellen, Taylor, 2001: 207		
ID|FBrf0144499
TP|abstract
|Drosophila meeting abstract
MABST|Recent studies have shown that the specification of neuronal identities is,
| in part, controlled by the combinatorial expression of transcription
| factors. Members of the LIM homeodomain (LIM-HD) and POU domain families of
| transcription factors are expressed in discrete subsets of developing
| neurons and have been shown in numerous organisms to regulate neuronal
| differentiation. Previous studies have demonstrated that two Drosophila
| LIM-HD members, islet( isl) and lim3, act in a combinatorial code to
| specify motor neuron subtype identity. Islet and Lim3 are co-expressed in a
| subset of CNS neurons including the TN and ISNb motor neurons. To identify
| factors that may act to differentiate between the TN and ISNb subgroups, we
| examined the expression pattern of characterized transcription factors. We
| found that Islet and Lim3 are co-expressed with the POU factor, Drifter, in
| the ISNb motor neuron subclass. Drifter expression is independent of Islet
| and Lim3 function indicating dfr is not a transcriptional target of these
| factors. To examine whether these proteins regulate similar aspects of
| motor axon targeting, we analyzed the ISNb nerve in trans -heterozygous
| combinations between dfr and isl and/ or lim3. Removing a single copy of
| isl, lim3 and dfr results in striking motor axon targeting defects
| characterized by reductions in muscle innervation. Specifically, the
| failure to innervate muscle cleft 12 and 13 observed in both isl 37Aa /+;
| dfr B129 /+ and lim3 Bd1 /+; dfr B129 /+ trans-heterozygotes is the most
| common phenotype of isl and lim3 mutant embryos. To further elucidate Dfr's
| role in the specification of ISNb motor neurons, we reduced the amount of
| Dfr protein through UAS-dfrdsRNA and UAS-dfr DN transgenes. Reducing Dfr
| activity causes the ISNb motor axons to leave the ventral muscle field and
| instead target the TN. In addition, misexpressing Dfr in the TN neurons
| results in a redirection of TN motor axons to the ISNb muscle target field.
| These studies suggest that Dfr may function in combination with Isl and
| Lim3 to specify muscle target selection by the ISNb motor neuron subclass.
AU|Certel
|S.J.
AU|Johnson
|W.A.
AU|Thor
|S.
YR|2001
TI|Regulation of motor axon targeting by the combinatorial activity of POU and LIM homeodomain proteins.
JR|Bellen, Taylor, 2001
PG|207
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144500	AU 1 Chen et al.	YR 1 2001	TP 1 Abstract	TI 1 Distinctive translation roles for alternative 5-UTRs in Drosophila peroxiredoxin I.	REFM 1 Bellen, Taylor, 2001: 149		
ID|FBrf0144500
TP|abstract
|Drosophila meeting abstract
MABST|Peroxiredoxin I, also discussed as nature killer cell enhance factor A and
| proliferation associate gene A, exists in organisms from E. coli to human
| and functions as antioxidant. In general, Peroxiredoxin I functions at
| least four biological incidents, i nclude thioredoxin redutase, kinase
| inhibitor, apoptosis regulator, and proliferation regulator, and also
| capable of influencing for differentiation, human immunodeficiency virus
| infection, organs transplant ischemia/ reperfusion, and skeleton
| development. In previously studies, expressing of Peroxiredoxin I mRNA was
| observed that can induced by oxidative agents and localized between central
| nervous system. In Drosophila, Peroxiredoxin I homologous gene was been
| cloned by 2D PAGE technique and validated as t hioredoxin redutase. We
| scanned expressing sequence tag datebase and found that Drosophila
| Peroxiredoxin I contains two transcriptional forms of mRNAs. Here we
| present an investigation of the mechanism of functional 5'-untranslation
| regions in Drosophila Peroxiredoxin I. In this study, we show that
| Drosophila Peroxiredoxin I contains two transcriptional forms of mRNAs that
| subsist in immensely amount in vivo. The biological functions of 5
| '-untranslation region, like efficient translation element and IRES
| activity were also presence individually in this study. The specific
| 5'-untranslation region element driven reporter lines was established and
| inspected of both reactive oxygen species and NO synthesis agents. The
| analysis shown that each 5'-untranslation region plays distinct but
| synergistic regulating role response the cellular oxidative and NO stress
| to either increase or decrease expressing of following reporter gene.
| Accordingly, the results suggest that the 5 '-untranslation regions of
| Drosophila Peroxiredoxin I play not only translation regulating events but
| also emergency roles in Drosophila central nervous system.
AU|Chen
|C.W.
AU|Lee
|D.F.
AU|Chang
|C.Y.
AU|Juang
|J.L.
YR|2001
TI|Distinctive translation roles for alternative 5-UTRs in Drosophila peroxiredoxin I.
JR|Bellen, Taylor, 2001
PG|149
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144501	AU 1 Cheng et al.	YR 1 2001	TP 1 Abstract	TI 1 Fasciclin II is required for the formation of odor memories.	REFM 1 Bellen, Taylor, 2001: 98		
ID|FBrf0144501
TP|abstract
|Drosophila meeting abstract
MABST|From an enhancer detection screen for genes expressed preferentially in the
| mushroom bodies, we isolated one line in which the enhancer detector was
| inserted into the first non-coding exon of the fasII gene. fasII encodes
| cell adhesion molecules of the immunoglobulin superfamily.
| Immunohistochemical analysis of Fas II expression confirmed that the
| protein products are concentrated along the axons of the a/ b neurons of
| mushroom bodies. Additional hypomorphic fasII mutants were generated via
| imprecise excision of the enhancer detector. The mutants have normal
| sensory functions (odor avoidance, electric shock avoidance, and odor
| avoidance after electric shock) and normal mushroom body neuron morphology,
| revealed by both light and electron micr oscopic analyses. The fasII rd1
| and fasII rd2 mutants show significantly lower memory than control flies at
| multiple times after olfactory classical conditioning. The performance
| deficit observed immediately after training is fully rescued by inducing a
| hs-fasII transgene with elevated temperature. Furthermore, the rescue of
| early memory can be reversed by switching off the transgene with reduced
| temperature. These experiments argue strongly for a role for Fas II in the
| physiology of mushroom body neurons underlying odor learning. We further
| dissected the role of Fas II by asking whether it serves memory formation,
| memory stability, or memory retrieval. When initial memory performance of
| the mutant is normalized to control animals by over-training, the mut ant
| and control flies exhibit an identical memory decay rate, arguing that
| memory stability is normal in the mutants. Induction of a hs-fasII
| transgene after training but just before testing fails to rescue
| performance, arguing that retrieval functions are not disrupted. These
| results indicate that Fas II is required for memory acquisition, but not
| memory stability or retrieval.
AU|Cheng
|Y.
AU|Endo
|K.
AU|Wu
|K.H.
AU|Davis
|R.
YR|2001
TI|Fasciclin II is required for the formation of odor memories.
JR|Bellen, Taylor, 2001
PG|98
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144502	AU 1 Chern and Choi	YR 1 2001	TP 1 Abstract	TI 1 Lobe is required for domain-specific growth of Drosophila eye disc.	REFM 1 Bellen, Taylor, 2001: 123		
ID|FBrf0144502
TP|abstract
|Drosophila meeting abstract
MABST|Notch (N) activation at the dorsoventral (DV) boundary of the Drosophila eye
| is essential for the growth of the eye. From the DV boundary a growth
| signal is then sent out and interpreted by cells of the dorsal and ventral
| domains. However, the identity of the growth signal and the domain-specific
| effector remain unknown. The Lobe (L) gene is one of the candidate genes
| involved in domain-specific growth. It was first identified in 1925 by
| mutations that preferentially abolish the ventral eye growth. However,
| mechanisms underlying the ventral-specific growth defect is little
| understood. Here we report cloning and characterization of the L gene
| function. L is a novel protein expressed preferentially in undifferentiated
| cells in the eye disc. L is required prior to differentiation to mediate
| the proliferative effect of activated N signaling, and this mediation is
| required only in the ventral domain. Furthermore, L regulates the ventral
| expression of a N ligand, Serrate (Ser), which has a novel function in
| controlling tissue growth. Relations among N, L and Ser may constitute a
| feedback mechanism that regulates N activity. We have also found that loss
| of L causes a ventral-specific, non-autonomous loss of tissue, suggesting
| that L regulates expression of diffusible growth-promoting factor in the
| ventral eye primordium. Together L and Ser present a molecular mechanism
| downstream of N that governs the ventral eye growth independently from
| dorsal eye development.
AU|Chern
|J.
AU|Choi
|K.W.
YR|2001
TI|Lobe is required for domain-specific growth of Drosophila eye disc.
JR|Bellen, Taylor, 2001
PG|123
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144503	AU 1 Cho et al.	YR 1 2001	TP 1 Abstract	TI 1 A model of habituation in Drosophila.	REFM 1 Bellen, Taylor, 2001: 99		
ID|FBrf0144503
TP|abstract
|Drosophila meeting abstract
MABST|Our laboratory has established a method for digitized tracking and anlysis
| of Drosophila movement at a fine resolution. Using this technique we are
| studying the behavioral response of flies to various odors including
| alcohol, an olfactory stimulus abundantly found in the natural environment
| of Drosophila. We have discovered that flies will transiently increase
| locomotor activity within a few seconds of exposure to ethanol vapor.
| Removal of the antennae abolishes this transient hyperlocomotioin. We term
| this olfactory mediated response "startle" as it is an immediate response
| to an olfactory stimulus. With repeated discrete exposures, this startle
| attenuates. This attenuation is reversible by a dishabituating mechanical
| stimulus and is not due to the accumulation of ethanol in the organism. By
| classical criteria, this behavior models habituation, a form of
| nonassociative learning whereby an organism learns to ignore
| inconsequential stimuli. We have modified this behavioral assay for high
| throughput and are screening through a collection of p[ Gal4] enahncer trap
| lines. Several mutants with either decreased or enhanced habituation have
| been identified in this assay. Using this forward genetic approach, we hope
| to discover novel mechanisms of behavioral plasticity in a simple model organism.
AU|Cho
|W.
AU|Wolf
|F.W.
AU|Heberlein
|U.
YR|2001
TI|A model of habituation in Drosophila.
JR|Bellen, Taylor, 2001
PG|99
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144504	AU 1 Choi et al.	YR 1 2001	TP 1 Abstract	TI 1 Electrophysiological and morphological characterization of motorneurons the intact ventral ganglion of third instar Drosophila larvae.	REFM 1 Bellen, Taylor, 2001: 249		
ID|FBrf0144504
TP|abstract
|Drosophila meeting abstract
MABST|To study the properties and modulation of neurons involved in the larval
| neuromuscular system, whole cell patch recordings were performed on ventral
| ganglion neurons. Motorneurons were readily identified with a neuron
| subtype-specific GAL4 line (C164; a gift of Vivian Budnik) driving GFP. The
| neurons studied show stereotypical patterns of activity and morphology that
| allow them to be individually identified within a given hemisegment.
| Concurrent rhodamine fills of specific neurons show that muscle innervation
| by a single neuron is reproducible with regard to the identity of the
| muscle innervated and bouton type. Somatic spikes were recorded from MN6/
| 7-Ib and MNISN-Is (nomenclature of Hoang and Chiba, 2001) neurons under
| current cl amp. The appearance of first spike is significantly delayed and
| the initiation of spike requires larger current amplitude in Is compared to
| Ib cells. Dual recordings at the neuromuscular junction (neuron/ muscle)
| reveal excitatory junction potentials evoked by single neurons. Dual
| recordings within the ventral ganglion (neuron/ neuron) imply a patterned
| circuitry that governs larval movement.
AU|Choi
|J.C.
AU|Park
|D.
AU|Griffith
|L.C.
YR|2001
TI|Electrophysiological and morphological characterization of motorneurons the intact ventral ganglion of third instar Drosophila larvae.
JR|Bellen, Taylor, 2001
PG|249
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144505	AU 1 Chou and Gusella	YR 1 2001	TP 1 Abstract	TI 1 Analysis of a Drosophila homolog of human DYT1 associated with primary torsion dystonia.	REFM 1 Bellen, Taylor, 2001: 183		
ID|FBrf0144505
TP|abstract
|Drosophila meeting abstract
MABST|The primary torsion dystonia is the most severe form of dystonia, a movement
| disorder. A dominant mutation which causes a glutamate codon deletion at
| the 3 prime end of DYT1 gene, mapped to human chromosome 9, has been found
| to account for most cases of the disease. DYT1 encodes torsinA, which
| appears to be a novel member of a protein superfamily of ATPases associated
| with diverse cellular activities (AAA+). A drosophila homolog of DYT1 gene
| has been identified which shows identity of 36% with torsinA along the
| entire region but showing over 70% identity at several functional motifs
| including the walker A and B ATP-binding domains. We have generated a few
| constructs carrying various forms of mutated fly torsin which presumably
| will disrupt normal function in dominant negative manners. The
| overexpression patterns of these constructs in S2 cells as well as eye
| phenotypes in transgenic flies will be discussed. This work will lay the
| foundation to establish a genetic screen to identify genes that potentially
| modify torsinA's effects and thereby to develop effective treatments for dystonia.
AU|Chou
|J.C.
AU|Gusella
|J.
YR|2001
TI|Analysis of a Drosophila homolog of human DYT1 associated with primary torsion dystonia.
JR|Bellen, Taylor, 2001
PG|183
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144506	AU 1 Chow et al.	YR 1 2001	TP 1 Abstract	TI 1 Functional characterization of Drosophila amphiphysin.	REFM 1 Bellen, Taylor, 2001: 23		
ID|FBrf0144506
TP|abstract
|Drosophila meeting abstract
MABST|In vertebrates, amphiphysin (amph) is hypothesized to act as a scaffolding
| protein during synaptic vesicle (SV) endocytosis. However, this model is
| based primarily on in vitro studies. To define the role of amph in vivo, we
| are conducting studies using Drosophila as a model organism. Molecular
| characterization of Drosophila amph reveals multiple isoforms of the
| protein that are highly related at the N-and C-termini. However, consensus
| sequences for binding to other endocytic proteins, such as clathrin, are
| absent. To study amph function in Drosophila, we have taken several
| approaches, including the production of antibodies for biochemical studies,
| and the generation of mutant flies. Using an antibody generated against
| full-length amph, we have found that several amph isoforms are widely
| expressed in diverse tissues throughout development. In embryos, amph is
| localized to epithelial cells and the gut, while in larvae, amph is
| localized to the CNS, imaginal discs and muscle. Immunofluorescent staining
| with pre-and postsynaptic markers at the larval neuromuscular junction
| (NMJ) indicate that amph is postsynaptic. To explore amph function in vivo,
| we have generated mutant flies. Null mutants are viable, but sluggish, and
| show no defects in synaptic morphology or synaptic physiology at the NMJ.
| Amph mutants, however, do demonstrate deficiencies in locomotion compared
| with controls of the same genetic background. These surprising results
| indicate that amph is not required for viability or SV endocytosis at the
| Drosophila larval NMJ. We are currently undertaking several genetic and
| biochemical screens to identify amph interacting proteins. The discovery of
| novel protein partners for amph may reveal functions for amph beyond its
| putative role at the synapse.
AU|Chow
|B.M.
AU|Leventis
|P.A.
AU|Stewart
|B.A.
AU|Boulianne
|G.L.
YR|2001
TI|Functional characterization of Drosophila amphiphysin.
JR|Bellen, Taylor, 2001
PG|23
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144507	AU 1 Chung and Kernan	YR 1 2001	TP 1 Abstract	TI 1 NompA, a ZP-domain extracellular matrix protein, forms part of mechanical linkage between mechanosensory neuron and cuticular structure.	REFM 1 Bellen, Taylor, 2001: 124		
ID|FBrf0144507
TP|abstract
|Drosophila meeting abstract
MABST|Mutations in the no-mechanoreceptor-potential A (nompA) gene disrupt
| mechanosensory transduction in Drosophila. nompA encodes a extracellular
| matrix protein with a ZP domain and several PAN modules; it is expressed
| specifically in each type I sense organ by the support cell that ensheaths
| the neuronal sensory process. Immunostaining and GFP-tagged fusion proteins
| showed that NompA is deposited in the dendrite cap at the apical tip of the
| sensory process. In nompA mutants, the dendrite cap is severely
| disorganized and detached from external cuticular structures and the
| sensory nerve endings. Thus NompA is required in the dendritic cap to
| transmit mechanical stimuli to the transduction apparatus. However, its
| specific role in the cap is still uncertain. To explore this, we have made
| transgenic flies that express various modified NompA proteins in wild type
| and mutant backgrounds. Analyses of these lines will be presented.
AU|Chung
|Y.D.
AU|Kernan
|M.
YR|2001
TI|NompA, a ZP-domain extracellular matrix protein, forms part of mechanical linkage between mechanosensory neuron and cuticular structure.
JR|Bellen, Taylor, 2001
PG|124
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144508	AU 1 Clements et al.	YR 1 2001	TP 1 Abstract	TI 1 Identification of transcriptional targets of eyeless required for neuronal differentiation.	REFM 1 Bellen, Taylor, 2001: 184		
ID|FBrf0144508
TP|abstract
|Drosophila meeting abstract
MABST|The Pax-6 homolog eyeless has been shown to have an essential role in the
| development of the protocerebrum in Drosophila. The gene is expressed in
| the developing and adult optic lobes, mushroom bodies, and central complex.
| The essential role of eyeless in these structures is supported by the brain
| defects observed in recently characterized eyeless mutants. We are focusing
| on the role of eyeless in the mushroom bodies. These neuropiles are
| involved in processing olfactory information and learning and memory. The
| expression of eyeless in mature mushroom body neurons (Kenyon cells), the
| partial or complete loss of these cells in eyeless mutants, and the
| aberrant morphology of the mutant Kenyon cells suggest that eyeless is
| required in mushroom body neuronal differentiation. We hypothesize that
| eyeless regulates a variety of target genes that are required for the
| acquisition and maintenance of neuronal characteristics. We have identified
| several target genes of eyeless whose function is required in postmitotic
| neurons via a genetic screen. In this screen, we analyzed the effects of
| elevated levels of Eyeless protein on reporter gene expression levels. A
| number of these putative target genes have been verified by yeast-1-hybrid
| analysis. We are currently characterizing several of these confirmed target
| genes to better understand their roles in the Drosophila brain and their
| relationship with eyeless.
AU|Clements
|J.
AU|Gafford
|B.
AU|Callaerts
|P.
YR|2001
TI|Identification of transcriptional targets of eyeless required for neuronal differentiation.
JR|Bellen, Taylor, 2001
PG|184
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144509	AU 1 Curtin et al.	YR 1 2001	TP 1 Abstract	TI 1 Gap junction genes are required for the formation of functional chemical synaptic connections in the visual system.	REFM 1 Bellen, Taylor, 2001: 94		
ID|FBrf0144509
TP|abstract
|Drosophila meeting abstract
MABST|Gap junctions have been observed between pre-and post synaptic neurons in
| several experimental systems, but their functional import has never been
| determined. Here, we will present evidence that gap junctions are essential
| precursors for the formation of functional chemical synaptic connections in
| the visual system. Mutants in the Drosophila gap junction ( innexin) genes,
| shakingB ( shB) and optic ganglia reduced (ogre), show defective chemical
| synaptic transmission between the retina and lamina. Both proteins are
| required during pupal development for normal synaptic connections to form.
| Further, ogre is required presynaptically while shB is required
| postsynaptically. This raises the interesting possibility that gap
| junctions form between retina and lamina cells during development as a
| necessary step in formation of functional chemical synapses. Specifically,
| shB and ogre shows reduced/ absent transients in the electroretinalgram
| (ERG). The ERG defect of ogre can be functionally separated from it's
| reduced optic ganglia phenotype. Mosaics in which only the eyes are mutant
| for ogre show this ERG phenotype. In addition, ogre ERGs can be rescued by
| driving ogre expression with sev-Gal4 and elav-Gal4 without rescuing the
| optic ganglia phenotype. These experiments also show that ogre is requi red
| in photoreceptors for normal ERGs. ShB's ERG defect is rescued by driving
| shB( N) expression via elav-Gal4 driver, but not a sev-Gal4 or GMR-Gal4,
| suggesting that shB( N) is required in the lamina. It may also be required
| in the retina. Both proteins are expressed in the visual system during the
| first half of pupal development when chemical synapses form. Both also need
| to be expressed during pupal development for rescue. Lasly, both mutants
| lead to minor errors in axonal projections of R1-8. For shB these defects
| are seen only in a minority of animals and for the most part pathfinding is
| normal in shB. These defects are more noticeable in ogre mutant eye animals.
AU|Curtin
|K.D.
AU|Zhang
|Z.
AU|Wyman
|R.J.
YR|2001
TI|Gap junction genes are required for the formation of functional chemical synaptic connections in the visual system.
JR|Bellen, Taylor, 2001
PG|94
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144510	AU 1 Curtin et al.	YR 1 2001	TP 1 Abstract	TI 1 Gap junction genes are not created equal: Mapping protein regions needed to promote functional chemical synaptic connections in visual system.	REFM 1 Bellen, Taylor, 2001: 24		
ID|FBrf0144510
TP|abstract
|Drosophila meeting abstract
MABST|Temporary gap junctions (GJs) have been observed between pre-and
| post-synaptic neurons. Recently, we showed that GJs are a necessary
| precursor to the formation of functional chemcial synatic connections in
| the Drosophila visual system. Mutations in two Drosophila GJ genes
| (innexins), shakingB (shB) and optic ganglia reduced (ogre), lead to a loss
| of transients in the electroretinogram (ERG) indicative of synaptic failure
| between the retina and lamina. Ogre is required presynaptically and shB( N)
| postsynaptically. Both act during development. Innexins are a large family.
| However, despite their high sequence homology, functional differences have
| been reported. Some form homotypic GJs while others do not. Others form
| heteromeric junctions. Voltage gating properties also vary. The biological
| implications of innexin differences have not been explored. Here we ask if
| innexins are interchangeable in promoting functional chemical synapses in
| flies. Specifically, we tested several innexins for their ability to rescue
| shB and ogre mutant ERGs and found that, by and large, innexins are not
| interchangeable. We mapped the protein regions required for this
| specificity by making chimeras between shB( N) and ogre and testing their
| ability to rescue both mutants. Each chimera rescued either shB or ogre,
| but never both. Specificity in GJ formation or function could contribute to
| chemical synaptic specificity by regulating which neurons couple and what
| signals they exchange. Cells may couple only if their innexins can mate
| with each other. The partially overlapping expression patterns of several
| innexins make this "mix and match" model of GJ formation a possibility.
AU|Curtin
|K.D.
AU|Zhang
|Z.
AU|Wyman
|R.J.
YR|2001
TI|Gap junction genes are not created equal: Mapping protein regions needed to promote functional chemical synaptic connections in visual system.
JR|Bellen, Taylor, 2001
PG|24
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144511	AU 1 Dauwalder et al.	YR 1 2001	TP 1 Abstract	TI 1 The takeout gene is controlled by the sex determination pathway and interacts with Fru in male courtship.	REFM 1 Bellen, Taylor, 2001: 100		
ID|FBrf0144511
TP|abstract
|Drosophila meeting abstract
MABST|Sex determination is controlled by a hierarchy of regulatory genes
| culminating with the sex-specific transcription factors doublesex and
| fruitless. These terminal factors are believed to regulate the sex-specific
| expression of numerous target genes that participate in sexual
| differentiation and sex-specific behavior. However, few of these target
| genes have yet been identified. In a subtractive hybridization screen
| directed at identifying sex-specific genes expressed in fly heads we
| identified several novel male-specific transcripts. One of the transcripts
| identified derives from the takeout gene, a factor concurrently identified
| as a circadian-regulated factor involved in the starvation response.
| Sequence comparisons reveal that takeout defines a novel gene family with
| at least twenty different members in the Drosophila genome. The proteins in
| this family seem to be secreted and to have limited similarity to factors
| known to bind lipophiles. We find that under non-starvation conditions
| takeout is expressed almost exclusively in the fat bodies of male heads and
| in subsets of cells in the antennae and the maxillary palp. Expression of
| takeout is under the control of the sex-determination pathway as shown by
| its activation in tra-2 mutant diplo-X individuals. In males, both dsx and
| fru activate expression of takeout, whereas in females dsx is involved in
| repressing the gene. Expression of the female-specific TRA protein under
| the control of the takeout promoter reduces the courtship index in male
| flies, demonstrating that the male identity of takeout expressing cells is
| important for normal courtship behavior. Furthermore, fru heterozygous
| males which are mutant for takeout show a reduction in courtship,
| suggesting that takeout interacts with the fru pathway in male courtship.
AU|Dauwalder
|B.
AU|Tsujimoto
|S.
AU|Moss
|J.
AU|Mattox
|W.
YR|2001
TI|The takeout gene is controlled by the sex determination pathway and interacts with Fru in male courtship.
JR|Bellen, Taylor, 2001
PG|100
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144512	AU 1 Yu et al.	YR 1 2001	TP 1 Abstract	TI 1 Transgenically-supplied fluorescent indicators of the physiological responses of neurons in the Drosophila brain.	REFM 1 Bellen, Taylor, 2001: 82		
ID|FBrf0144512
TP|abstract
|Drosophila meeting abstract
MABST|The learning of odors and the expression of odor memories requires the
| participation of mushroom body neurons. Despite the identification of the
| relevant neurons along with a handful of required genes and proteins, there
| remains no readily available method for monitoring the physiological state
| of these neurons. Such methodology is critical in order to understand the
| changes in neuronal physiology that occur with the formation,
| consolida-tion, and expression of odor memories. We have developed several
| UAS-transgenes that encode protein fusions of GFP with potential for
| monitor-ing in vivo changes in calcium level, membrane potential, and
| synaptic activity. These have been expressed in all mushroom body neurons
| or in selected sets of mushroom body neurons using the GAL4 system. Calcium
| responses of mushroom body neurons to ionic depolarization or stimulation
| with neurotransmitters have been monitored with camgaroos, which are
| insertions of calmodulin inside yellow mutants of GFP (Baird et al, PNAS
| 96: 11241-6, 1999; Griesbeck et al, J. Biol. Chem. in press, 2001).
| Camgaroos increase fluorescence acutely in response to elevations of
| calcium or pH. Strong depolarization with K + leads to a robust but
| transient increase in fluorescence of two different camgaroos. This
| response is not due to a change in intracellular pH from depolar-ization,
| since intracellular pH indicators reported a slight decrease in pH with
| depolarization. Fluorescence increases were attenuated by calcium channel
| blockers or by chelating extracellular calcium, indicating that the
| responses are due to calcium influx through voltage-dependent calcium
| channels. Acetylcholine (ACh) is the putative neurotransmitter released by
| antennal lobe relay neurons onto the dendrites of mushroom body neurons in
| the calyx. Application of ACh to the calyx produced a rapid and tran s-ient
| increase in fluorescence in the axons of mushroom body neurons but not in
| the cell bodies or dendrites. In addition, the calcium increases occurred
| in all three classes of mushroom body neurons, including the a/ b, a'/ b',
| and g neurons, showing that all mushroom body neurons respond to ACh
| stimulation. These increases were blocked with antagonists of nicotinic ACh
| receptors. Thus, all mushroom body neurons respond to ACh stimulation with
| activation of voltage-dependent calcium channels distributed along their
| axons. The validation of this system and establish-ment of these baseline
| properties now offer the possibility of monitoring in vivo in both normal
| or mutant animals, the changes in neuronal calcium that occur during
| behavioral conditioning, the administration of drugs, or the presentation
| of other types of environmental stimuli.
AU|Yu
|D.
AU|Baird
|G.S.
AU|Tsien
|R.Y.
AU|Davis
|R.L.
YR|2001
TI|Transgenically-supplied fluorescent indicators of the physiological responses of neurons in the Drosophila brain.
JR|Bellen, Taylor, 2001
PG|82
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144513	AU 1 Dean and Booker	YR 1 2001	TP 1 Abstract	TI 1 The role of dTRAFs 1 and 2 in Drosophila development.	REFM 1 Bellen, Taylor, 2001: 150		
ID|FBrf0144513
TP|abstract
|Drosophila meeting abstract
MABST|TRAFs (tumor necrosis factor receptor-associated factors) are important
| mediator proteins in the TNF/ NGF pathways. Through a conserved domain,
| these molecules bind to TNF/ NGF receptor complexes and act as adaptors,
| recruiting downstream pathways to the receptor by physically coupling them.
| Here, we describe the isolation and characterization of mutations in dtrafs
| 1 and 2 of Drosophila. Our results suggest a role for dtraf1 in larval
| growth and for dtraf2 in early embryogenesis.
AU|Dean
|D.M.
AU|Booker
|R.
YR|2001
TI|The role of dTRAFs 1 and 2 in Drosophila development.
JR|Bellen, Taylor, 2001
PG|150
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144514	AU 1 Rao et al.	YR 1 2001	TP 1 Abstract	TI 1 Neuropeptides affect an extremely diverse set of physiological processes.	REFM 1 Bellen, Taylor, 2001: 25		
ID|FBrf0144514
TP|abstract
|Drosophila meeting abstract
MABST|Neuropeptides affect an extremely diverse set of physiological processes.
| Neuropeptides are often coreleased with neurotransmitters and, unlike
| neurotransmitters, cells responding to neuropeptides may be distant from
| the site of secretion. Thus, it is often difficult to measure the amount of
| neuropeptide release in vivo by electrophysiological methods. Here we
| report the development of an in vivo system for studying the developmental
| expression, processing, transport, and release of neuropeptides. A
| GFP-tagged atrial natruiretic factor fusion (preproANF-EMD) was expressed
| in the Drosophila nervous system with the panneural promoter, elav. During
| embryonic development, proANF-EMD was first seen to accumulate in synaptic
| regions of the CNS in stage 17 embryos. By the third instar larval stage,
| highly fluorescent neurons were evident throughout the CNS and PNS. In the
| adult, fluorescence was pronounced in the mushroom bodies, antennal lobe,
| and the central complex. At the larval neuromuscular junction, proANF-EMD
| was concentrated in nerve terminals. We compared the release of proANF-EMD
| from synaptic boutons of NMJ 6/ 7 which contain almost exclusively
| glutamate containing clear vesicles to those of NMJ 12 which include the
| peptidergic type III boutons. Upon depolarization, approximately 60% of the
| tagged neuropeptide was released from NMJs of both muscles in 15 minutes.
| Although the elav promoter is uniformly active in the Drosophila nervous
| system, NMJ 12, prior to stimulation, contained on average 46-fold more
| neuropeptide than did NMJ 6/ 7, and thus, NMJ 12 released much more
| proANF-EMD during stimulation. Our results suggest that peptidergic neurons
| have an enhanced ability to accumulate neuropeptides as compared to neurons
| that primarily release classical neurotransmitters.
AU|Rao
|S.
AU|Lang
|C.
AU|Levitan
|E.S.
AU|Deitcher
|D.L.
YR|2001
TI|Neuropeptides affect an extremely diverse set of physiological processes.
JR|Bellen, Taylor, 2001
PG|25
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144515	AU 1 Demidenko et al.	YR 1 2001	TP 1 Abstract	TI 1 Regulated nuclear export of the homeodomain transcription factor Prospero.	REFM 1 Bellen, Taylor, 2001: 151		
ID|FBrf0144515
TP|abstract
|Drosophila meeting abstract
MABST|Subcellular distribution of the Prospero protein is dynamically regulated
| during Drosophila nervous system development. Prospero is first detected in
| neuroblasts where it becomes cortically localized and tethered by the
| adapter protein, Miranda. After division, Prospero enters the nucleus of
| daughter ganglion mother cells where it functions as a tr anscription
| factor. We have identified a novel Prospero allele, which produces a
| protein lacking the C-terminal 30 amino acids of the highly conserved
| Prospero domain. This results in the protein remaining in the cytoplasm of
| ganglion mother cells. Molecular dissection of the homeo -and Prospero
| domains, and expression of chimeric Prospero proteins in mammalian and
| insect cells indicates that Prospero contains a nuclear export signal that
| is masked by the Prospero domain. Nuclear export signal of Prospero, which
| is sensitive to the drug Leptomycin B, is mediated by Exportin.
| Site-directed mutagenesis shows that the conserved hydrophobic residues of
| the Prospero nuclear export signal Leu1252, Leu1257, Leu1262 or Phe1264 are
| essential for its export activity, and the tertiary structure of Prospero
| may regulate its export. Mutation of the nuclear export signal-mask in
| Drosophila embryos prevents Prospero nuclear localization in ganglion
| mother cells. We propose that a combination of cortical tethering and
| regulated nuclear export controls Prospero subcellular distribution and
| function in all higher eukaryotes.
AU|Demidenko
|Z.N.
AU|Badenhorst
|P.
AU|Jones
|T.
AU|Bi
|X.
AU|Mortin
|M.A.
YR|2001
TI|Regulated nuclear export of the homeodomain transcription factor Prospero.
JR|Bellen, Taylor, 2001
PG|151
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144516	AU 1 Desai	YR 1 2001	TP 1 Abstract	TI 1 Neural RPTPs may form inhibitory heterodimers.	REFM 1 Bellen, Taylor, 2001: 208		
ID|FBrf0144516
TP|abstract
|Drosophila meeting abstract
MABST|In Drosophila, at least five RPTPs are highly expressed by neurons and
| function to help developing CNS, motor and/ or retinal axons reach their
| synaptic targets. Genetic analysis reveals that two of these RPTPs, DLAR
| and PTP99A function antagonistically at a specific axonal choice point. The
| ISNb nerve bypasses its ventrolateral muscle (VLM) targets in Dlar mutants
| but innervates the VLM in Dlar: Ptp99A double mutants, indicating that DLAR
| normally functions to inhibit or counteract PTP99A during ISNb axon
| outgrowth. Experiments involving the structure and function of the
| cytoplasmic domains of vertebrate RPTPs suggest that some RPTPs may form
| inhibitory homodimers. Although inhibitory heterodimer formation between
| DLAR and PTP99A is an attractive model to explain these genetic results,
| neither hetero-nor homodimer formation have been directly detected in
| Drosophila. Here we report the identification of a novel Ptp69D mutant
| whose phenotypes can also be explained by the formation of inhibitory RPTP
| heterodimers. Ptp69D 7A2 homozygote embryos have a much more severe
| phenotype than that of Ptp69D( ÿ) null embryos. The motor axon defects
| conferred by Ptp69D 7A2 phenocopy those seen in Dlar, Ptp69D double mutants
| whereas the CNS defects are similar to those seen in Ptp10D; Ptp69D double
| mutants. Furthermore, these defects are dose-dependent, with the phenotype
| of Ptp69D 7A2 > Ptp69D 7A2 /Ptp69D( ÿ) > Ptp69D( ÿ). These results
| suggest that the protein encoded by Ptp69D 7A2 poisons both DLAR and
| PTP10D. Both motor and central axon defects can be suppressed by increasing
| the expression of PTP99A and enhanced by reducing the expression of PTP10D.
| These results are consistent with the interpretation that PTP69D 7A2
| interacts directly with DLAR, PTP10D and PTP99A and that this interaction
| inactivates DLAR and PTP10D.
AU|Desai
|C.
YR|2001
TI|Neural RPTPs may form inhibitory heterodimers.
JR|Bellen, Taylor, 2001
PG|208
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144517	AU 1 Deshpande and Urban	YR 1 2001	TP 1 Abstract	TI 1 The role of yan in the development of the embryonic CNS.	REFM 1 Bellen, Taylor, 2001: 152		
ID|FBrf0144517
TP|abstract
|Drosophila meeting abstract
MABST|Different cell types in the Drosophila central nervous system (CNS) are
| formed from a relatively few precursor cells, the neuroblasts (NBs), which
| delaminate from the neurogenic region of the ectoderm. The delamination
| occurs in five waves, S1-S5, finally leading to a subepidermal layer
| consisting of about 30 NBs, each with a unique identity, arranged in a
| stereotyped spatial pattern in each hemisegment. This information depends
| on several factors such as the concentrations of various morphogens,
| cell-cell interactions and long range signals present at the position and
| time of its birth. The early NBs, delaminating during S1 and S2, form an
| orthogonal array of four rows (2/ 3,4,5,6/ 7) and three columns (medial,
| intermediate, and lateral). However, the three column and four
| row-arrangement pattern is only transitory during early stages of
| neurogenesis which is obscured by late emerging (S3-S5) neuroblasts.
| Therefore the aim of our study has been to identify novel genes which play
| a role in the formation or specification of late delaminating NBs. A
| genetic screen in collaboration with the Dr. C Kl”mbt was done to identity
| novel and yet unidentified genes in the process of late neuroblast
| formation and specification. We found NB 7-3, a late delaminating
| neuroblast, to be missing in one of the mutant stocks which was later found
| to localise on the gene anterior open or yan. This gene encodes a
| transcription factor that functions as a negative regulator of cell
| differentiation and proliferation. Here we present data regarding the role
| of yan in context to the Notch signalling pathway in CNS development, as we
| find that the embryonic mutant phenotype of Notch is suppressed by the yan
| mutation. Further, ectopic expression of activated Yan in the neuroectoderm
| mimics a neurogenic phenotype. The cause of this neurogenic phenotype seems
| to due to the down regulation of the expression of the Notch target,
| Enhancer of split (E( spl)). Thus, we hypothesise that yan is responsible
| for maintaining the cells of the neuroectoderm in an undifferentiated state
| by counter acting the Notch signal thereby promoting neural fate.
AU|Deshpande
|N.
AU|Urban
|J.
YR|2001
TI|The role of yan in the development of the embryonic CNS.
JR|Bellen, Taylor, 2001
PG|152
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144518	AU 1 Dobritsa et al.	YR 1 2001	TP 1 Abstract	TI 1 The steroidogenic gene dare plays roles in nervous system development, maintenance and function.	REFM 1 Bellen, Taylor, 2001: 125		
ID|FBrf0144518
TP|abstract
|Drosophila meeting abstract
MABST|Steroid hormones play important roles in the development and function of the
| nervous system in both invertebrates and vertebrates. Little is known about
| the source of steroids that participate in these processes. An interesting
| possibility is that steroid hormones are synthesized within the brain and
| act locally to modulate nervous system functions. The Drosophila mutant
| dare has defects in steroid synthesis, as well as in the maturation and
| function of the nervous system. Cloning of the dare gene reveal ed that it
| encodes a homologue of the mammalian enzyme adrenodoxin reductase, which is
| required for the biosynthesis of steroid hormones. An allelic series has
| been generated for dare, and the resulting alleles have a variety of
| phenotypes. The hypomorphic dare 1 mutant, which contains a P element
| insertion, has abnormal responses to olfactory and visual stimuli. Null
| alleles have molting defects and undergo second instar lethality.
| Intermediate allelic combinations show a delay of pupariation, severe
| uncoordination, and significant and widespread degeneration of the adult
| nervous system, suggesting that dare in required to maintain the integrity
| of the nervous system. All of the defects are fully rescued by a transgenic
| copy of dare. At least some of the abnormalities of dare mutants, such as
| defects in molting and pupariation, can be rescued by feeding mutants the
| insect steroid hormone ecdysone, thus providing evidence that the
| production of steroids is in fact affected in dare. Overexpression of dare
| within the nervous system (in all or particular subsets of neurons, but not
| in glia) rescues dare-induced neurodegeneration but does not have an effect
| on other mutant phenotypes, such as defects in female fertility, thus
| suggesting the possibility that steroids can be produced and can function
| locally within the nervous system of Drosophila. To see if dare is involved
| in the development of the nervous system, and also to examine the autonomy
| of dare function, we performed mosaic analysis of the fly eyes. We found
| that dare is indeed required for eye development and that it functions
| there in a cell-autonomous manner.
AU|Dobritsa
|A.A.
AU|Freeman
|M.R.
AU|Carlson
|J.R.
YR|2001
TI|The steroidogenic gene dare plays roles in nervous system development, maintenance and function.
JR|Bellen, Taylor, 2001
PG|125
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144519	AU 1 Dobritsa et al.	YR 1 2001	TP 1 Abstract	TI 1 Odor receptor expression and olfactory coding in Drosophila.	REFM 1 Bellen, Taylor, 2001: 7		
ID|FBrf0144519
TP|abstract
|Drosophila meeting abstract
MABST|A family of candidate odorant receptor (DOR) genes has recently been
| identified in Drosophila. It includes about 60 members predicted to encode
| G-protein coupled receptors. DOR genes are expressed in neurons of two
| olfactory organs: the third antennal segment and the maxillary palp. A
| major problem in this system is to determine the functional organization of
| receptor gene expression. How does the expression of individual receptors
| among the neurons of the olfactory system, as determined by molecular
| means, correlate with the electrophysiological responses of these neurons
| to individual odors? Odorant receptors are expected to localize to the
| dendrites of olfactory receptor neurons (ORNs). To determine the
| subcellular localization of DOR proteins, we raised an antibody predicted
| to recognize two closely related family members expressed in the antenna,
| DOR 22a and 22b. Immunofluorescence labeling shows that these proteins are
| localized within a subset of olfactory sensilla on antenna, exactly as
| expected for an odorant receptor expressed in the dendrites. ImmunoEM
| analysis confirmed that the antibody indeed labels the dendritic membrane.
| The sensilla stained with the antibody belong to a particular morphological
| class, the large sensilla basiconica. There are three physiologically
| distinct subtypes among this class, known as ab1, ab2, and ab3. To find out
| in which physiological subtype the DOR 22a gene is expressed, we have
| created a line expressing GAL4 under the control of the DOR 22a promoter.
| When this line is crossed with the UAS-GFP reporter line, GFP fluorescence
| is found in the subset of sensilla corresponding to those in which the
| endogenous DOR 22a gene is expressed. We performed electrophysiological
| single-unit recordings on the GFP -labelled sensilla, and determined that
| all 22a-expressing sensilla belong to the physiological class ab3. To find
| out in which of the two ORNs in the ab3 sensilla the 22a receptor is
| present, we are killing or inactivating the DOR 22a-expressing neurons. We
| have also linked expression of another gene, DOR 85e, to a particular
| functional type of ORNs. This gene is expressed in the maxillary palps, and
| using similar kind of analysis we found that it is expressed in the pb1A
| ORNs, which respond strongly to ethyl acetate. A maxillary palp contains
| only 6 functional types of ORNs, and thus this approach should enable us to
| construct an integrated molecular and physiological map for this olfactory organ.
AU|Dobritsa
|A.A.
AU|Warr
|C.G.
AU|van der Goes van Naters
|W.
AU|Steinbrecht
|R.A.
AU|Carlson
|J.R.
YR|2001
TI|Odor receptor expression and olfactory coding in Drosophila.
JR|Bellen, Taylor, 2001
PG|7
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144520	AU 1 Drier et al.	YR 1 2001	TP 1 Abstract	TI 1 Memory enhancement by a mammalian atypical PKC isoform, PKMz in D. melanogaster.	REFM 1 Bellen, Taylor, 2001: 101		
ID|FBrf0144520
TP|abstract
|Drosophila meeting abstract
MABST|Synaptic stimulation can activate signal-transduction pathways, producing
| persistently active protein kinases, and these have been attractive
| candidate components of memory mechanisms. PKMz is a truncated,
| persistently activated isoform of an atypical protein kinase C (aPKCz),
| which lacks the N-terminal pseudosubstrate regulatory domain. We used a
| Pavlovian olfactory learning paradigm in Drosophila to examine the role of
| PKMz in memory formation. We find that induction of the mouse PKMz (MaPKMz)
| transgene enhances memory. This enhancement requires persistent kinase
| activity, since induction of neither a full-length nor a kinase-dead
| transgene produces this effect. The MaPKMz-mediated enhancement is
| temporally specific: it is optimal if the transgene is induced 30 minutes
| after training and does not occur if induced prior to, or more than 2 hours
| post-training. An atypical PKC has been identified in Drosophila, and
| Western blots as well a s kinase activity assays indicate that the M-form
| of this kinase is present and active in Drosophila heads. As with the mouse
| homologue, induction of a transgene encoding the putative M-form of the
| Drosophila aPKC also enhances memory. We also find that both chelerythrine,
| an inhibitor of PKM activity, and induction of a dominant-negative MaPKMz
| transgene inhibit memory without affecting learning. Thus, aPKM is
| necessary for normal memory maintenance and is sufficient to enhance this
| process. The temporal specificity leads us to speculate that aPKM is part
| of, or is acted upon, by the synaptic tag.
AU|Drier
|E.A.
AU|Cowan
|M.
AU|Tello
|M.K.
AU|Wu
|P.
AU|Blace
|N.
AU|Sacktor
|T.C.
AU|Yin
|J.C.P.
YR|2001
TI|Memory enhancement by a mammalian atypical PKC isoform, PKMz in D. melanogaster.
JR|Bellen, Taylor, 2001
PG|101
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144521	AU 1 Dubnau and Tully	YR 1 2001	TP 1 Abstract	TI 1 Functional anatomy of olfactory memory: Dissection of spatial and temporal requirements for neurotransmission during memory consolidation.	REFM 1 Bellen, Taylor, 2001: 102		
ID|FBrf0144521
TP|abstract
|Drosophila meeting abstract
MABST|Lesion experiments usually result in irreversible brain damage, which has
| limited their use for dissecting the temporally and mechanistically
| distinct processes of acquisition, storage and memory retrieval. By using a
| Gal4 driven temperature -sensitive shibire transgene to disrupt synaptic
| transmission reversibly and on the time-scale of minutes, we have
| investigated the temporal and spatial requirements for ongoing neural
| activity during memory formation. By transiently disrupting synaptic
| activity in several relevant anatomical loci, we demonstrate distinct
| temporal and spatial requirements for synaptic transmission during
| acquisition, consolidation and retrieval of olfactory memory.
AU|Dubnau
|J.
AU|Tully
|T.
YR|2001
TI|Functional anatomy of olfactory memory: Dissection of spatial and temporal requirements for neurotransmission during memory consolidation.
JR|Bellen, Taylor, 2001
PG|102
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144522	AU 1 Caldwell et al.	YR 1 2001	TP 1 Abstract	TI 1 Effects of chordotonal mutants on larval locomotion.	REFM 1 Bellen, Taylor, 2001: 126		
ID|FBrf0144522
TP|abstract
|Drosophila meeting abstract
MABST|Chordotonal organs (CHO) underlie hearing and proprioception in the
| Drosophila adult. Mutations that disrupt adult CHO function are likely to
| affect larval CHOs as well; in fact one CHO mutant, touch-insensitive larva
| B (tilB), was first identified by larval insensitivity to touch. We have
| found that other CHO mutants are similarly touch-insensitive, including
| atonal (ato), beethoven (btv), smetana (smet) and 5D10. We wanted determine
| whether larval CHO function may provide sensory feedback during locomotion.
| By staining CHO mutants with monoclonal antibody 22C10 (pan-neural) we
| documented morphological defects in number, position and orientation in the
| lateral pentascolopidial organs of the larval abdominal segments. Using
| DIAS (Dynamic Image Analysis System) software, we next analyzed larval
| locomotor patterns. This software tracks, frame-by-frame, the paths taken
| by third instar wandering larvae in parameters such as speed, acceleration
| and direction change. This analysis has shown severe defects in larval
| paths in CHO mutants as compared to the wild type. Furthermore, there are
| statistically significant differences between mutant and wild-type strains
| for speed and for direction change, but not for acceleration. Overall, we
| are able to demonstrate that CHO dysfunction is associated with aberrant
| larval locomotion.
AU|Caldwell
|J.C.
AU|Miller
|M.M.
AU|Wing
|S.
AU|Eberl
|D.F.
YR|2001
TI|Effects of chordotonal mutants on larval locomotion.
JR|Bellen, Taylor, 2001
PG|126
TP|abstract
}
# EOR
REFR
{
RETE|ID 1 FBrf0144523	AU 1 Elmore and Smith	YR 1 2001	TP 1 Abstract	TI 1 Subcellular localization and developmental expression of putative odor receptor OR43b.	REFM 1 Bellen, Taylor, 2001: 127		
ID|FBrf0144523
TP|abstract
|Drosophila meeting abstract
MABST|Two families of put