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Gene Review

Snap25  -  synaptosomal-associated protein 25

Mus musculus

Synonyms: Bdr, GENA 70, GENA70, SNAP-25, SUP, ...
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Disease relevance of Snap25


Psychiatry related information on Snap25


High impact information on Snap25


Chemical compound and disease context of Snap25


Biological context of Snap25

  • However, axonal growth and the early topographic arrangement of thalamocortical fiber pathways appear normal in the Snap25 KO, where action potential mediated synaptic vesicle release is disrupted [15].
  • Patch-clamp recordings in fetal Snap25-null mutant cortex demonstrated that ablation of SNAP-25 eliminated evoked GABA(A) receptor-mediated postsynaptic responses while leaving a low level of spontaneous AP-independent events intact, supporting the involvement of SNAP-25 in the regulated synaptic transmission of early developing GABAergic neurons [16].
  • In hippocampal cell cultures of wild-type mice, punctate staining of SNAP-25 colocalized with both GABAergic and glutamatergic synaptic markers, whereas stimulus-evoked vesicular recycling was abolished at terminals of both transmitter phenotypes in Snap25-/- neurons [16].
  • Spontaneous locomotor hyperactivity in a mouse mutant with a deletion including the Snap gene on chromosome 2 [1].
  • Analysis of genomic DNA revealed that the Snap gene dosage in Cm/+ mice was 50% lower than control littermates [1].

Anatomical context of Snap25

  • The gene encoding the synaptosomal-associated protein--25 kDa (SNAP-25) was mapped by analysis of somatic cell hybrids and an intersubspecies backcross to mouse Chromosome 2 [1].
  • These findings suggest that rabphilin is involved in the docking step of regulated exocytosis in PC12 cells, possibly through interaction between the C2B domain and SNAP-25 [17].
  • The C2B domain of rabphilin directly interacts with SNAP-25 and regulates the docking step of dense core vesicle exocytosis in PC12 cells [17].
  • These results show that Ca2+ modulates dynamic docking of granules to the plasma membrane and that this process is due to a Ca2+-dependent interaction between SNAP-25 and Synaptotagmin 1 [18].
  • Our results thus provide evidence that SNAP-25 is critical for evoked GABA release during development and is expressed in the presynaptic terminals of mature GABAergic neurons, consistent with its function as a component of a fundamental core SNARE complex required for stimulus-driven neurotransmission [16].

Associations of Snap25 with chemical compounds

  • Members of the SNARE (soluble N -ethylmaleimide-sensitive fusion protein attachment protein receptor) superfamily [syntaxins, VAMPs (vesicle-associated membrane proteins) and SNAP25 (synaptosome-associated protein-25)-related proteins] are required for intracellular membrane-fusion events in eukaryotes [19].
  • The predicted amino acid sequence also includes a cluster of four closely spaced cysteine residues, similar to the metal binding domains of some metalloproteins, suggesting that the SNAP-25 polypeptide may have the potential to coordinately bind metal ions [20].
  • Removal of cholesterol in the plasma membrane by methyl-beta-cyclodextrin facilitated both redistribution of ECFP-SNAP25 and sequential exocytosis by threefold [21].
  • Thus, the relative expression levels of SNAP-25 and SNAP-23 might control the mode (regulated vs. basal) of granule release by forming docking complexes at different Ca(2+) thresholds [22].
  • We report that the increased raft association of SNAP-23 occurs due to the substitution of a highly conserved phenylalanine residue present in SNAP-25 with a cysteine residue [23].

Physical interactions of Snap25

  • Interestingly, we found that SNARE motif-exposed syntaxin 1A mutants were retained in endoplasmic reticulum (ER) and failed to transport to the cell surface in the absence of SNAP-25, suggesting that the exposure of the SNARE motif causes ER retention and complexation with SNAP-25 helps the ER escape [24].
  • Moreover, both alpha1A isoforms form part of the P/Q-channels-SNARE complexes in situ because they are coimmunoprecipitated from solubilized chromaffin cell membranes by a monoclonal SNAP-25 antibody [25].
  • Mouse taste cells with G protein-coupled taste receptors lack voltage-gated calcium channels and SNAP-25 [26].

Co-localisations of Snap25

  • However, during the first stages of the cell transdifferentiation process, SNAP-25 migrates alone out to the developing growth cone and what will become the nerve endings and varicosities of the mature neurites; alpha1A follows and colocalizes to SNAP-25 in the now mature processes [25].

Regulatory relationships of Snap25


Other interactions of Snap25

  • Differential control of the releasable vesicle pools by SNAP-25 splice variants and SNAP-23 [7].
  • In the docking assay, addition of Ca2+ induces the formation of a SNAP-25-Synaptotagmin 1 complex [18].
  • In neurons, assembly of SNARE core complexes comprising the presynaptic membrane-associated SNAREs syntaxin 1 and SNAP25, and the vesicle-associated SNARE VAMP2, is necessary for synaptic vesicle exocytosis [19].
  • One such factor, Snapin, has been reported to be a brain-specific protein that interacts with SNAP25, and regulates association of the putative Ca2+-sensor synaptotagmin with the synaptic SNARE complex [Ilardi, Mochida and Sheng (1999) Nat. Neurosci. 2, 119-124] [19].
  • Disruption of the gene encoding SNAP-25, a component of the soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor complex required for regulated neuroexocytosis, eliminates evoked but not spontaneous neurotransmitter release (Washbourne et al., 2002) [29].
  • From these results, we conclude that progesterone-progesterone receptor-mediated SNAP25 expression in cumulus oocyte complexes and granulosa cells regulates cytokine and chemokine secretion via an exocytosis system [30].

Analytical, diagnostic and therapeutic context of Snap25


  1. Spontaneous locomotor hyperactivity in a mouse mutant with a deletion including the Snap gene on chromosome 2. Hess, E.J., Jinnah, H.A., Kozak, C.A., Wilson, M.C. J. Neurosci. (1992) [Pubmed]
  2. Mouse model of hyperkinesis implicates SNAP-25 in behavioral regulation. Hess, E.J., Collins, K.A., Wilson, M.C. J. Neurosci. (1996) [Pubmed]
  3. Cleavage of SNAP-25 and VAMP-2 impairs store-operated Ca2+ entry in mouse pancreatic acinar cells. Rosado, J.A., Redondo, P.C., Salido, G.M., Sage, S.O., Pariente, J.A. Am. J. Physiol., Cell Physiol. (2005) [Pubmed]
  4. Distribution of synaptosomal-associated protein 25 in nerve growth cones and reduction of neurite outgrowth by botulinum neurotoxin A without altering growth cone morphology in dorsal root ganglion neurons and PC-12 cells. Morihara, T., Mizoguchi, A., Takahashi, M., Kozaki, S., Tsujihara, T., Kawano, S., Shirasu, M., Ohmukai, T., Kitada, M., Kimura, K., Okajima, S., Tamai, K., Hirasawa, Y., Ide, C. Neuroscience (1999) [Pubmed]
  5. Molecular characterization of MPT83: a seroreactive antigen of Mycobacterium tuberculosis with homology to MPT70. Hewinson, R.G., Michell, S.L., Russell, W.P., McAdam, R.A., Jacobs, W.R. Scand. J. Immunol. (1996) [Pubmed]
  6. The hyh mutation uncovers roles for alpha Snap in apical protein localization and control of neural cell fate. Chae, T.H., Kim, S., Marz, K.E., Hanson, P.I., Walsh, C.A. Nat. Genet. (2004) [Pubmed]
  7. Differential control of the releasable vesicle pools by SNAP-25 splice variants and SNAP-23. Sørensen, J.B., Nagy, G., Varoqueaux, F., Nehring, R.B., Brose, N., Wilson, M.C., Neher, E. Cell (2003) [Pubmed]
  8. The neuron-specific kinesin superfamily protein KIF1A is a unique monomeric motor for anterograde axonal transport of synaptic vesicle precursors. Okada, Y., Yamazaki, H., Sekine-Aizawa, Y., Hirokawa, N. Cell (1995) [Pubmed]
  9. An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming. Richmond, J.E., Weimer, R.M., Jorgensen, E.M. Nature (2001) [Pubmed]
  10. Transgenic rescue of SNAP-25 restores dopamine-modulated synaptic transmission in the coloboma mutant. Steffensen, S.C., Henriksen, S.J., Wilson, M.C. Brain Res. (1999) [Pubmed]
  11. Coloboma mouse mutant as an animal model of hyperkinesis and attention deficit hyperactivity disorder. Wilson, M.C. Neuroscience and biobehavioral reviews. (2000) [Pubmed]
  12. Cholesterol oxidation reduces Ca(2+)+MG (2+)-ATPase activity, interdigitation, and increases fluidity of brain synaptic plasma membranes. Wood, W.G., Igbavboa, U., Rao, A.M., Schroeder, F., Avdulov, N.A. Brain Res. (1995) [Pubmed]
  13. Recombinant SNAP-25 is an effective substrate for Clostridium botulinum type A toxin endopeptidase activity in vitro. Ekong, T.A., Feavers, I.M., Sesardic, D. Microbiology (Reading, Engl.) (1997) [Pubmed]
  14. Genotoxicity evaluation of buprofezin, petroleum oil and profenofos in somatic and germ cells of male mice. Fahmy, M.A., Abdalla, E.F. Journal of applied toxicology : JAT. (1998) [Pubmed]
  15. Choreography of early thalamocortical development. Molnár, Z., Higashi, S., López-Bendito, G. Cereb. Cortex (2003) [Pubmed]
  16. Expression and function of SNAP-25 as a universal SNARE component in GABAergic neurons. Tafoya, L.C., Mameli, M., Miyashita, T., Guzowski, J.F., Valenzuela, C.F., Wilson, M.C. J. Neurosci. (2006) [Pubmed]
  17. The C2B domain of rabphilin directly interacts with SNAP-25 and regulates the docking step of dense core vesicle exocytosis in PC12 cells. Tsuboi, T., Fukuda, M. J. Biol. Chem. (2005) [Pubmed]
  18. SNAP-25 and synaptotagmin 1 function in Ca2+-dependent reversible docking of granules to the plasma membrane. Chieregatti, E., Witkin, J.W., Baldini, G. Traffic (2002) [Pubmed]
  19. Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells. Buxton, P., Zhang, X.M., Walsh, B., Sriratana, A., Schenberg, I., Manickam, E., Rowe, T. Biochem. J. (2003) [Pubmed]
  20. The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations. Oyler, G.A., Higgins, G.A., Hart, R.A., Battenberg, E., Billingsley, M., Bloom, F.E., Wilson, M.C. J. Cell Biol. (1989) [Pubmed]
  21. Sequential exocytosis of insulin granules is associated with redistribution of SNAP25. Takahashi, N., Hatakeyama, H., Okado, H., Miwa, A., Kishimoto, T., Kojima, T., Abe, T., Kasai, H. J. Cell Biol. (2004) [Pubmed]
  22. SNAP-23 functions in docking/fusion of granules at low Ca2+. Chieregatti, E., Chicka, M.C., Chapman, E.R., Baldini, G. Mol. Biol. Cell (2004) [Pubmed]
  23. The SNARE proteins SNAP-25 and SNAP-23 display different affinities for lipid rafts in PC12 cells. Regulation by distinct cysteine-rich domains. Salaün, C., Gould, G.W., Chamberlain, L.H. J. Biol. Chem. (2005) [Pubmed]
  24. Domain requirement for the membrane trafficking and targeting of syntaxin 1A. Yang, X., Xu, P., Xiao, Y., Xiong, X., Xu, T. J. Biol. Chem. (2006) [Pubmed]
  25. Dynamic association of the Ca2+ channel alpha1A subunit and SNAP-25 in round or neurite-emitting chromaffin cells. Andrés-Mateos, E., Renart, J., Cruces, J., Solís-Garrido, L.M., Serantes, R., de Lucas-Cerrillo, A.M., Aldea, M., García, A.G., Montiel, C. Eur. J. Neurosci. (2005) [Pubmed]
  26. Mouse taste cells with G protein-coupled taste receptors lack voltage-gated calcium channels and SNAP-25. Clapp, T.R., Medler, K.F., Damak, S., Margolskee, R.F., Kinnamon, S.C. BMC Biol. (2006) [Pubmed]
  27. Neuromuscular transmission and muscle contractility in SNAP-25-deficient coloboma mice. Adler, M., Sheridan, R.E., Deshpande, S.S., Oyler, G.A. Neurotoxicology (2001) [Pubmed]
  28. SNAP25, but not syntaxin 1A, recycles via an ARF6-regulated pathway in neuroendocrine cells. Aikawa, Y., Xia, X., Martin, T.F. Mol. Biol. Cell (2006) [Pubmed]
  29. Normal development of embryonic thalamocortical connectivity in the absence of evoked synaptic activity. Molnár, Z., López-Bendito, G., Small, J., Partridge, L.D., Blakemore, C., Wilson, M.C. J. Neurosci. (2002) [Pubmed]
  30. Synaptosomal-associated protein 25 gene expression is hormonally regulated during ovulation and is involved in cytokine/chemokine exocytosis from granulosa cells. Shimada, M., Yanai, Y., Okazaki, T., Yamashita, Y., Sriraman, V., Wilson, M.C., Richards, J.S. Mol. Endocrinol. (2007) [Pubmed]
  31. Separate populations of receptor cells and presynaptic cells in mouse taste buds. DeFazio, R.A., Dvoryanchikov, G., Maruyama, Y., Kim, J.W., Pereira, E., Roper, S.D., Chaudhari, N. J. Neurosci. (2006) [Pubmed]
  32. Inhibition of SNAP-25 phosphorylation at Ser187 is involved in chronic morphine-induced down-regulation of SNARE complex formation. Xu, N.J., Yu, Y.X., Zhu, J.M., Liu, H., Shen, L., Zeng, R., Zhang, X., Pei, G. J. Biol. Chem. (2004) [Pubmed]
  33. SNAP-25 is essential for cortical granule exocytosis in mouse eggs. Ikebuchi, Y., Masumoto, N., Matsuoka, T., Yokoi, T., Tahara, M., Tasaka, K., Miyake, A., Murata, Y. Am. J. Physiol. (1998) [Pubmed]
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