The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

SNAP25  -  synaptosomal-associated protein, 25kDa

Bos taurus

This record was replaced with 540853.
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of SNAP25


High impact information on SNAP25

  • The alpha-SNAP-SNARE complex can bind NSF, and NSF-dependent hydrolysis of ATP dissociates the complex, separating syntaxin, SNAP-25, and VAMP [2].
  • Thus we assign a dual role to SNAP-25 and suggest that its nine C-terminal amino acids are directly involved in coupling the calcium sensor to the final step in exocytosis [3].
  • Plasma membrane disruptions are resealed by an active molecular mechanism thought to be composed, in part, of kinesin, CaM kinase, snap-25, and synaptobrevin [4].
  • Kinetics of single granule fusions from cells expressing truncated forms showed slow onset and decay times when compared with control cells expressing full SNAP-25 [5].
  • Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses [6].

Biological context of SNAP25

  • Synthetic peptides patterned after the C-terminus of synaptosomal associated protein of 25 kDa (SNAP25) efficiently abrogate regulated exocytosis [7].
  • In contrast, the use of SNAP25 N-terminal-derived peptides to modulate SNAP receptors (SNARE) complex assembly and neurosecretion has not been explored [7].
  • We conclude that a small domain of the SNAP-25 C terminus and its counterpart in synaptobrevin play an essential role in the final membrane fusion step of exocytosis [8].
  • Point mutations in the C-terminal domain of SNAP-25 (K201E and L203E) produced a marked inhibition of secretion, whereas single (Q174K, Q53K) and double mutants (Q174K/Q53K) of amino acids from the so-called zero layer only produced a moderate alteration in secretion [8].
  • Fusion proteins made of green fluorescent protein coupled to SNAP-25 or synaptobrevin were overexpressed in bovine chromaffin cells in order to study the role of critical protein domains in exocytosis [8].

Anatomical context of SNAP25


Associations of SNAP25 with chemical compounds


Physical interactions of SNAP25

  • In this study, we examined whether G0 controls such dissociation of the SNAP-25/VAMP-2 complex in the regulation of priming [16].

Regulatory relationships of SNAP25


Other interactions of SNAP25

  • Our study reveals that, in the absence of calcium, native synaptotagmin 1 binds the t-SNARE heterodimer, formed from syntaxin and SNAP-25 [13].
  • A complex of rab3A, SNAP-25, VAMP/synaptobrevin-2 and syntaxins in brain presynaptic terminals [19].
  • Basal expression of SNAP-25 was also modified by the protein kinase C (PKC) activator, phorbol 12-myristate 13-acetate, but not by Gö6976, a PKC-alpha inhibitor, suggesting that the Ca(2+)-insensitive PKC-epsilon isoform control basal expression of SNAP-25 in these cells [20].

Analytical, diagnostic and therapeutic context of SNAP25


  1. Exocytotic mechanism studied by truncated and zero layer mutants of the C-terminus of SNAP-25. Wei, S., Xu, T., Ashery, U., Kollewe, A., Matti, U., Antonin, W., Rettig, J., Neher, E. EMBO J. (2000) [Pubmed]
  2. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Söllner, T., Bennett, M.K., Whiteheart, S.W., Scheller, R.H., Rothman, J.E. Cell (1993) [Pubmed]
  3. Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity. Xu, T., Binz, T., Niemann, H., Neher, E. Nat. Neurosci. (1998) [Pubmed]
  4. Vesicle accumulation and exocytosis at sites of plasma membrane disruption. Miyake, K., McNeil, P.L. J. Cell Biol. (1995) [Pubmed]
  5. A single amino acid near the C terminus of the synaptosomeassociated protein of 25 kDa (SNAP-25) is essential for exocytosis in chromaffin cells. Criado, M., Gil, A., Viniegra, S., Gutiérrez, L.M. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  6. Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses. Schiavo, G., Stenbeck, G., Rothman, J.E., Söllner, T.H. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  7. Small peptides patterned after the N-terminus domain of SNAP25 inhibit SNARE complex assembly and regulated exocytosis. Blanes-Mira, C., Merino, J.M., Valera, E., Fernández-Ballester, G., Gutiérrez, L.M., Viniegra, S., Pérez-Payá, E., Ferrer-Montiel, A. J. Neurochem. (2004) [Pubmed]
  8. Modifications in the C terminus of the synaptosome-associated protein of 25 kDa (SNAP-25) and in the complementary region of synaptobrevin affect the final steps of exocytosis. Gil, A., Gutiérrez, L.M., Carrasco-Serrano, C., Alonso, M.T., Viniegra, S., Criado, M. J. Biol. Chem. (2002) [Pubmed]
  9. High affinity interaction of syntaxin and SNAP-25 on the plasma membrane is abolished by botulinum toxin E. Rickman, C., Meunier, F.A., Binz, T., Davletov, B. J. Biol. Chem. (2004) [Pubmed]
  10. Subcellular localization of chromogranins, calcium channels, amine carriers, and proteins of the exocytotic machinery in bovine splenic nerve. Leitner, B., Lovisetti-Scamihorn, P., Heilmann, J., Striessnig, J., Blakely, R.D., Eiden, L.E., Winkler, H. J. Neurochem. (1999) [Pubmed]
  11. SNAP-25 is present on chromaffin granules and acts as a SNAP receptor. Tagaya, M., Genma, T., Yamamoto, A., Kozaki, S., Mizushima, S. FEBS Lett. (1996) [Pubmed]
  12. A peptide that mimics the carboxy-terminal domain of SNAP-25 blocks Ca(2+)-dependent exocytosis in chromaffin cells. Gutiérrez, L.M., Cànaves, J.M., Ferrer-Montiel, A.V., Reig, J.A., Montal, M., Viniegra, S. FEBS Lett. (1995) [Pubmed]
  13. Mechanism of calcium-independent synaptotagmin binding to target SNAREs. Rickman, C., Davletov, B. J. Biol. Chem. (2003) [Pubmed]
  14. Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and permeabilized chromaffin cells: correlation with its blockade of catecholamine release. Foran, P., Lawrence, G.W., Shone, C.C., Foster, K.A., Dolly, J.O. Biochemistry (1996) [Pubmed]
  15. Differential contribution of syntaxin 1 and SNAP-25 to secretion in noradrenergic and adrenergic chromaffin cells. Baltazar, G., Tomé, A., Carvalho, A.P., Duarte, E.P. Eur. J. Cell Biol. (2000) [Pubmed]
  16. Regulation of the priming of exocytosis and the dissociation of SNAP-25 and VAMP-2 in adrenal chromaffin cells. Misonou, H., Ohara-Imaizumi, M., Kumakura, K. Neurosci. Lett. (1997) [Pubmed]
  17. Peptides that mimic the carboxy-terminal domain of SNAP-25 block acetylcholine release at an Aplysia synapse. Apland, J.P., Biser, J.A., Adler, M., Ferrer-Montiel, A.V., Montal, M., Canaves, J.M., Filbert, M.G. Journal of applied toxicology : JAT. (1999) [Pubmed]
  18. Mitogen-activated protein kinase is activated by Ca(2+) entry through L- and N-type channels and regulates Ca(2+)-induced SNAP-25 expression. Mendoza, I., Tonk, E., Díaz-Raya, P., Cárdenas, A.M. Ann. N. Y. Acad. Sci. (2002) [Pubmed]
  19. A complex of rab3A, SNAP-25, VAMP/synaptobrevin-2 and syntaxins in brain presynaptic terminals. Horikawa, H.P., Saisu, H., Ishizuka, T., Sekine, Y., Tsugita, A., Odani, S., Abe, T. FEBS Lett. (1993) [Pubmed]
  20. Distinct protein kinases regulate SNAP-25 expression in chromaffin cells. Montiel, C., Mendoza, I., García, C.J., Awad, Y., García-Olivares, J., Solís-Garrido, L.M., Lara, H., García, A.G., Cárdenas, A.M. J. Neurosci. Res. (2003) [Pubmed]
  21. Multiple forms of SNARE complexes in exocytosis from chromaffin cells: effects of Ca(2+), MgATP and botulinum toxin type A. Lawrence, G.W., Dolly, J.O. J. Cell. Sci. (2002) [Pubmed]
  22. SNAP-25 is present in a SNARE complex in adrenal chromaffin cells. Roth, D., Burgoyne, R.D. FEBS Lett. (1994) [Pubmed]
  23. Adrenal chromaffin cells contain functionally different SNAP-25 monomers and SNAP-25/syntaxin heterodimers. Höhne-Zell, B., Gratzl, M. FEBS Lett. (1996) [Pubmed]
WikiGenes - Universities