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Gene Review

Snap25  -  Synaptosomal-associated protein 25kDa

Drosophila melanogaster

Synonyms: CG17676, CG17884, CG40452, Dmel\CG40452, SNAP-25, ...
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High impact information on Snap25

  • The neuronal SNARE complex is formed via the interaction of synaptobrevin with syntaxin and SNAP-25 [1].
  • We have isolated a SNAP-25 temperature-sensitive paralytic mutant in Drosophila, SNAP-25(ts) [2].
  • In neurons, the t-SNARE SNAP-25 is essential for synaptic vesicle fusion but its exact role in this process is unknown [2].
  • Evolutionary conservation of synaptosome-associated protein 25 kDa (SNAP-25) shown by Drosophila and Torpedo cDNA clones [3].
  • None of the SNAP-25 sequences has a membrane-spanning region, but all contain a cluster of cysteine residues that can be palmitoylated for membrane attachment [3].

Biological context of Snap25

  • In this study, we performed a mutagenesis screen to identify new SNAP-25 alleles that fail to complement our previously isolated recessive temperature-sensitive allele of SNAP-25, SNAP-25(ts) [4].

Anatomical context of Snap25


Analytical, diagnostic and therapeutic context of Snap25


  1. Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly. Littleton, J.T., Chapman, E.R., Kreber, R., Garment, M.B., Carlson, S.D., Ganetzky, B. Neuron (1998) [Pubmed]
  2. Two distinct effects on neurotransmission in a temperature-sensitive SNAP-25 mutant. Rao, S.S., Stewart, B.A., Rivlin, P.K., Vilinsky, I., Watson, B.O., Lang, C., Boulianne, G., Salpeter, M.M., Deitcher, D.L. EMBO J. (2001) [Pubmed]
  3. Evolutionary conservation of synaptosome-associated protein 25 kDa (SNAP-25) shown by Drosophila and Torpedo cDNA clones. Risinger, C., Blomqvist, A.G., Lundell, I., Lambertsson, A., Nässel, D., Pieribone, V.A., Brodin, L., Larhammar, D. J. Biol. Chem. (1993) [Pubmed]
  4. A Drosophila SNAP-25 null mutant reveals context-dependent redundancy with SNAP-24 in neurotransmission. Vilinsky, I., Stewart, B.A., Drummond, J., Robinson, I., Deitcher, D.L. Genetics (2002) [Pubmed]
  5. SNAP-24, a Drosophila SNAP-25 homologue on granule membranes, is a putative mediator of secretion and granule-granule fusion in salivary glands. Niemeyer, B.A., Schwarz, T.L. J. Cell. Sci. (2000) [Pubmed]
  6. Cysteine-string proteins: a cycle of acylation and deacylation? Gundersen, C.B., Umbach, J.A., Mastrogiacomo, A. Life Sci. (1996) [Pubmed]
  7. Complex gene organization of synaptic protein SNAP-25 in Drosophila melanogaster. Risinger, C., Deitcher, D.L., Lundell, I., Schwarz, T.L., Larhammar, D. Gene (1997) [Pubmed]
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