Differential expression of transcripts from syb, a Drosophila melanogaster gene encoding VAMP (synaptobrevin) that is abundant in non-neuronal cells

Chin, AC; Burgess, Robert W.; Wong, Brian; Schwarz, Thomas L.; Scheller, RH

doi:10.1016/0378-1119(93)90291-a

Cited by 53 publications

(29 citation statements)

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“…The homology of syb with vertebrate synaptobrevins strongly suggests a role in fusion at the plasma membrane. Syb is also widespread within the organism and is not concentrated at the synapse (20,21). As described here, loss of syb in a somatic clone of cells is lethal.…”

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confidence: 84%

Members of the synaptobrevin/vesicle-associated membrane protein (VAMP) family in Drosophila are functionally interchangeable in vivo for neurotransmitter release and cell viability

Bhattacharya

Stewart

Niemeyer

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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Synaptobrevins or VAMPs are vesicle-associated membrane proteins, often called v-SNARES, that are important for vesicle transport and fusion at the plasma membrane. Drosophila has two characterized members of this gene family: synaptobrevin (syb) and neuronal synaptobrevin (n-syb). Mutant phenotypes and gene-expression patterns indicate that n-Syb is exclusively neuronal and required only for synaptic vesicle secretion, whereas Syb is ubiquitous and, as shown here, essential for cell viability. When the eye precursor cells were made homozygous for syb ؊ , the eye failed to develop. In contrast, n-syb ؊ eye clones developed appropriately but failed to activate downstream neurons. To determine whether the two proteins are structurally specialized to accomplish these distinct in vivo functions, we have driven the expression of each gene in the absence of the other to look for phenotypic rescue. We find that expression of n-syb during eye development can rescue the cell lethality of the syb mutations, as can rat VAMP2 and cellubrevin. Expression of syb can restore synaptic transmission to n-syb mutants as assayed both by electroretinogram and recordings of excitatory junctional currents at the neuromuscular junction. Therefore, we find that Syb, which usually is not involved in synaptic function, can mediate Ca 2؉ -triggered synaptic activity and that no particular specialization of the v-SNARE is required to differentiate synaptic exocytosis from other forms.

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confidence: 84%

Members of the synaptobrevin/vesicle-associated membrane protein (VAMP) family in Drosophila are functionally interchangeable in vivo for neurotransmitter release and cell viability

Bhattacharya

Stewart

Niemeyer

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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“…VAMP was first identified by screening a cDNA library of the Torpedo electric organ (Trimble et al, 1988) and later cloned from rat, bovine, human, Drosophila, yeast, squid, and Aplysia (Elferink et al, 1989;S0dhof et al, 1989;Archer et al, 1990;Chin et al, 1993;Di Antonio et al, 1993;Protopopov et al, 1993;Hunt et al, 1994;Yamasaki et al, 1994;Sweeney et al, 1995). Four regions can be identified in the primary structure of VAMP.…”

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confidence: 99%

“…Two isoforms of VAMP were identified in the nervous and neuro-endocrine tissues with dissimilar amino-terminal proline-rich domain part Elferink et al, 1989;Archer et al, 1990;Chin et al, 1993). In situ hybridization shows that they are differently distributed among the various brain regions (Trimble et al, 1991;Chin et al, 1993).…”

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VAMP/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues.

Rossetto

Gorza

Schiavo

et al. 1996

The Journal of Cell Biology

125

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Abstract. VAMP/synaptobrevin is part of the synaptic vesicle docking and fusion complex and plays a central role in neuroexocytosis. Two VAMP (vesicle-associated membrane protein) isoforms are expressed in the nervous system and are differently distributed among the specialized parts of the tissue. Here, VAMP-1 and -2 are shown to be present in all rat tissues tested, including kidney, adrenal gland, liver, pancreas, thyroid, heart, and smooth muscle. The two isoforms are differentially expressed in various tissues and their level may depend on differentiation. VAMP-1 is restricted to exocrine pancreas and to kidney tubular cells, whereas VAMP-2 is the predominant isoform present in Langerhans islets and in glomerular cells. Both isoforms show a patchy vesicular intracellular distribution in confocal microscopy. The present results provide evidence for the importance of neuronal VAMP proteins in the physiology of all cells.UKARYOTIC cells possess organized secretory pathways for the exocytosis of proteins and other molecules. These secretory routes consist of several discrete membrane compartments and of transport vesicles that shuttle between these compartments (Rothman and

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“…RD-SNAREs group only a number of "short VAMPs" or "brevins" (Filippini et al, 2001) such as (i) VAMP1, 2, 3, (ii) D. melanogaster SybA/B (expressed in the gut and malpighian tubules at early developmental stages) (Chin et al, 1993), (iii) D. melanogaster n-syb (functionally interchangeable in vivo with SybA/B for neurotransmitter release and cell viability) (Bhattacharya et al, 2002) and (iv) C. elegans Snb (essential for viability and required for functional synaptic transmission) (Nonet et al, 1998).…”

Section: Resultsmentioning

confidence: 99%

VAMP subfamilies identified by specific R-SNARE motifs

Rossi

Picco

Vacca

et al. 2004

Biology of the Cell

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In eukaryotes, interactions among the a-helical coiled-coil domains (CCDs) of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) play a pivotal role in mediating the fusion among vesicles and target membranes. Surface residues of such CCDs are major candidates to regulate the specificity of membrane fusion, as they may alter local charge at the interaction layers and surface of the fusion complex, possibly modulating its formation and/or the binding of non-SNARE regulatory factors. Based on alternate patterns in surface residues, we have identified two motifs which group vesicular SNAREs in two novel subfamilies: RG-SNAREs and RD-SNAREs. The RG-SNARE CCD is common to all members of the widely conserved family of long VAMPs or longins and to yeast and non-neuronal VAMPs, possibly mediating ″basic″ fusion mechanisms; instead, only synaptobrevins from Bilateria share an RD-SNARE CCD, which is likely to mediate interactions to specific, yet unknown, regulatory factors and/or be the landmark of rapid fusion reactions like that mediating the release of neurotransmitters.

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Differential expression of transcripts from syb, a Drosophila melanogaster gene encoding VAMP (synaptobrevin) that is abundant in non-neuronal cells

Cited by 53 publications

References 10 publications

Members of the synaptobrevin/vesicle-associated membrane protein (VAMP) family in Drosophila are functionally interchangeable in vivo for neurotransmitter release and cell viability

Members of the synaptobrevin/vesicle-associated membrane protein (VAMP) family in Drosophila are functionally interchangeable in vivo for neurotransmitter release and cell viability

VAMP/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues.

VAMP subfamilies identified by specific R-SNARE motifs

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