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Gene Review

SNAP23  -  synaptosomal-associated protein, 23kDa

Homo sapiens

Synonyms: HsT17016, SNAP-23, SNAP23A, SNAP23B, Synaptosomal-associated protein 23, ...
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Disease relevance of SNAP23

  • Within the syntaxin family, syntaxin 4 interacted with SNAP23 and all vesicle-associated membrane proteins (VAMPs) examined, except tetanus neurotoxin insensitive VAMP (TI-VAMP) [1].
  • Here we report the generation of isoform-specific antibodies to SNAP-23 cloned from human melanoma cells, and their use in detecting the expression and localization of the endogenous SNAP-23 protein in several tissues and cell lines [2].
  • Potential involvement of galectin-3 and SNAP23 in Aeromonas hydrophila cytotoxic enterotoxin-induced host cell apoptosis [3].

High impact information on SNAP23


Biological context of SNAP23


Anatomical context of SNAP23


Associations of SNAP23 with chemical compounds

  • Here, we have employed cysteine mutants of SNAP25/SNAP23, which have modified affinities for raft domains, to examine whether raft association of these proteins is important for the regulation of exocytosis [7].
  • A dominant-negative variant of SNAP-23 decreases the cell surface expression of the neuronal glutamate transporter EAAC1 by slowing constitutive delivery [14].
  • CFTR-mediated chloride currents are inhibited by introducing excess SNAP-23 into HT29-Cl.19A epithelial cells [6].
  • Antibodies against SNAP-23 inhibited Ca(++) and GTP-gamma-S-induced exocytosis of CD67-enriched specific granules, but they hardly affected exocytosis of the CD63-enriched azurophilic granules, when introduced into electropermeabilized neutrophils [15].
  • SNAP-23 cleavage is inhibited by calpeptin, calpastatin, calpain inhibitor IV, and E-64d, but not by caspase 3 inhibitor III or cathepsin inhibitor I. When tested for their effect on secretion, none of the calpain-specific inhibitors significantly affected release of soluble components from any of the three platelet granule storage pools [16].

Physical interactions of SNAP23

  • Expression of a dominant-negative variant of SNAP-23 that lacks a domain required for SNARE complex assembly decreased the fraction of EAAC1 found on the cell surface and decreased total EAAC1 expression, while two control constructs had no effect [14].
  • Conversely, CFTR activity is stimulated by a SNAP-23 antibody that blocks the binding of this t-SNARE to the CFTR amino-terminal tail [6].
  • In vitro binding studies established that SNAP-23 binds to syntaxin 6 [15].
  • Despite this, essentially all syntaxin 4 and most of VAMP-2 in these rafts were present in SNARE complexes containing SNAP-23, while essentially none of these complexes were present in nonraft membranes [17].

Regulatory relationships of SNAP23


Other interactions of SNAP23

  • We studied the N-terminal coiled-coil domain of SNAP-23 (SNAP-23N), a non-neuronal homologue of SNAP-25, and its interaction with other coiled-coil domains [21].
  • Third, E. chaffeensis also inhibited the gene transcription of RAB5A, SNAP23, and STX16, which are involved in membrane trafficking [22].
  • The dominant-negative variant of SNAP-23 also slowed the rate of EAAC1 delivery to the plasma membrane [14].
  • SNAP-23 physically associates with CFTR by binding to its amino-terminal tail, a region that modulates channel gating [6].
  • SNAP-23 was translocated to the cell surface, colocalizing with syntaxin 6, on neutrophil activation [15].

Analytical, diagnostic and therapeutic context of SNAP23


  1. Soluble NSF attachment protein receptors (SNAREs) in RBL-2H3 mast cells: functional role of syntaxin 4 in exocytosis and identification of a vesicle-associated membrane protein 8-containing secretory compartment. Paumet, F., Le Mao, J., Martin, S., Galli, T., David, B., Blank, U., Roa, M. J. Immunol. (2000) [Pubmed]
  2. Tissue distribution of SNAP-23 and its subcellular localization in 3T3-L1 cells. Wong, P.P., Daneman, N., Volchuk, A., Lassam, N., Wilson, M.C., Klip, A., Trimble, W.S. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  3. Potential involvement of galectin-3 and SNAP23 in Aeromonas hydrophila cytotoxic enterotoxin-induced host cell apoptosis. Galindo, C.L., Gutierrez, C., Chopra, A.K. Microb. Pathog. (2006) [Pubmed]
  4. Relocation of the t-SNARE SNAP-23 from lamellipodia-like cell surface projections regulates compound exocytosis in mast cells. Guo, Z., Turner, C., Castle, D. Cell (1998) [Pubmed]
  5. Asymmetric phospholipid distribution drives in vitro reconstituted SNARE-dependent membrane fusion. Vicogne, J., Vollenweider, D., Smith, J.R., Huang, P., Frohman, M.A., Pessin, J.E. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  6. CFTR chloride channels are regulated by a SNAP-23/syntaxin 1A complex. Cormet-Boyaka, E., Di, A., Chang, S.Y., Naren, A.P., Tousson, A., Nelson, D.J., Kirk, K.L. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  7. Lipid raft association of SNARE proteins regulates exocytosis in PC12 cells. Salaün, C., Gould, G.W., Chamberlain, L.H. J. Biol. Chem. (2005) [Pubmed]
  8. Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machinery. Faigle, W., Colucci-Guyon, E., Louvard, D., Amigorena, S., Galli, T. Mol. Biol. Cell (2000) [Pubmed]
  9. The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23. Diefenbach, R.J., Diefenbach, E., Douglas, M.W., Cunningham, A.L. Biochemistry (2002) [Pubmed]
  10. Genomic organization, chromosomal localization, alternative splicing, and isoforms of the human synaptosome-associated protein-23 gene implicated in vesicle-membrane fusion processes. Lazo, P.A., Nadal, M., Ferrer, M., Area, E., Hernández-Torres, J., Nabokina, S.M., Mollinedo, F., Estivill, X. Hum. Genet. (2001) [Pubmed]
  11. Expression of eosinophil target SNAREs as potential cognate receptors for vesicle-associated membrane protein-2 in exocytosis. Logan, M.R., Lacy, P., Bablitz, B., Moqbel, R. J. Allergy Clin. Immunol. (2002) [Pubmed]
  12. Combinatorial SNARE complexes modulate the secretion of cytoplasmic granules in human neutrophils. Mollinedo, F., Calafat, J., Janssen, H., Martín-Martín, B., Canchado, J., Nabokina, S.M., Gajate, C. J. Immunol. (2006) [Pubmed]
  13. Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues. Ravichandran, V., Chawla, A., Roche, P.A. J. Biol. Chem. (1996) [Pubmed]
  14. A dominant-negative variant of SNAP-23 decreases the cell surface expression of the neuronal glutamate transporter EAAC1 by slowing constitutive delivery. Fournier, K.M., Robinson, M.B. Neurochem. Int. (2006) [Pubmed]
  15. Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis. Martín-Martín, B., Nabokina, S.M., Blasi, J., Lazo, P.A., Mollinedo, F. Blood (2000) [Pubmed]
  16. SNAP-23 is a target for calpain cleavage in activated platelets. Rutledge, T.W., Whiteheart, S.W. J. Biol. Chem. (2002) [Pubmed]
  17. Ternary SNARE Complexes Are Enriched in Lipid Rafts during Mast Cell Exocytosis. Puri, N., Roche, P.A. Traffic (2006) [Pubmed]
  18. Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells. Low, S.H., Roche, P.A., Anderson, H.A., van Ijzendoorn, S.C., Zhang, M., Mostov, K.E., Weimbs, T. J. Biol. Chem. (1998) [Pubmed]
  19. Phosphorylation of SNAP-23 in activated human platelets. Polgár, J., Lane, W.S., Chung, S.H., Houng, A.K., Reed, G.L. J. Biol. Chem. (2003) [Pubmed]
  20. SNAP-29 is a promiscuous syntaxin-binding SNARE. Hohenstein, A.C., Roche, P.A. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  21. Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain. Freedman, S.J., Song, H.K., Xu, Y., Sun, Z.Y., Eck, M.J. J. Biol. Chem. (2003) [Pubmed]
  22. Survival strategy of obligately intracellular Ehrlichia chaffeensis: novel modulation of immune response and host cell cycles. Zhang, J.Z., Sinha, M., Luxon, B.A., Yu, X.J. Infect. Immun. (2004) [Pubmed]
  23. SNAP-23 participates in SNARE complex assembly in rat adipose cells. St-Denis, J.F., Cabaniols, J.P., Cushman, S.W., Roche, P.A. Biochem. J. (1999) [Pubmed]
  24. Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c. Araki, S., Tamori, Y., Kawanishi, M., Shinoda, H., Masugi, J., Mori, H., Niki, T., Okazawa, H., Kubota, T., Kasuga, M. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  25. Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane. Imai, A., Nashida, T., Yoshie, S., Shimomura, H. Arch. Oral Biol. (2003) [Pubmed]
  26. SNAP-23 in rat kidney: colocalization with aquaporin-2 in collecting duct vesicles. Inoue, T., Nielsen, S., Mandon, B., Terris, J., Kishore, B.K., Knepper, M.A. Am. J. Physiol. (1998) [Pubmed]
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