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Gene Review

Snap23  -  synaptosomal-associated protein 23

Rattus norvegicus

Synonyms: SNAP-23, Synaptosomal-associated protein 23, Vesicle-membrane fusion protein SNAP-23
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Disease relevance of Snap23


High impact information on Snap23


Biological context of Snap23


Anatomical context of Snap23


Associations of Snap23 with chemical compounds


Physical interactions of Snap23

  • Associated kinase activity, which diminishes after stimulation as a consequence of intracellular calcium increases, specifically phosphorylates syntaxin 4 thereby affecting its capacity to bind to its t-SNARE partner SNAP-23 [5].

Regulatory relationships of Snap23


Other interactions of Snap23

  • In the pancreatic acinar cell, synaptosomal-associated protein of 23 kd (SNAP-23) is the major SNAP-25 isoform expressed in pancreatic acinar cells, but its role in acinar cell exocytosis has not been determined [1].
  • Immunoblotting analysis showed that parotid acini contain both syntaxin-4 and SNAP-23, plausible candidates of target membranes (t-) SNAREs in non-neuronal cells [10].
  • Contrary to results from in vitro binding assays, SNAP-23 was found predominantly associated with syntaxin 3 [8].
  • SNAREs were found either excluded (syntaxin2), equally distributed between raft and non-raft fractions (syntaxin4, VAMP-8, VAMP-2), or selectively enriched in rafts (syntaxin3, SNAP-23) [11].
  • Cognate SNARE complexes of syntaxin3 with SNAP-23 and VAMP-8 were enriched in rafts, whereas Munc18-2/syntaxin3 complexes were excluded [11].

Analytical, diagnostic and therapeutic context of Snap23


  1. Cholecystokinin-regulated exocytosis in rat pancreatic acinar cells is inhibited by a C-terminus truncated mutant of SNAP-23. Huang, X., Sheu, L., Tamori, Y., Trimble, W.S., Gaisano, H.Y. Pancreas (2001) [Pubmed]
  2. Subcellular localization of tetanus neurotoxin-insensitive vesicle-associated membrane protein (VAMP)/VAMP7 in neuronal cells: evidence for a novel membrane compartment. Coco, S., Raposo, G., Martinez, S., Fontaine, J.J., Takamori, S., Zahraoui, A., Jahn, R., Matteoli, M., Louvard, D., Galli, T. J. Neurosci. (1999) [Pubmed]
  3. Phosphorylation of SNAP-23 regulates exocytosis from mast cells. Hepp, R., Puri, N., Hohenstein, A.C., Crawford, G.L., Whiteheart, S.W., Roche, P.A. J. Biol. Chem. (2005) [Pubmed]
  4. Cultured glial cells express the SNAP-25 analogue SNAP-23. Hepp, R., Perraut, M., Chasserot-Golaz, S., Galli, T., Aunis, D., Langley, K., Grant, N.J. Glia (1999) [Pubmed]
  5. SNAREs and associated regulators in the control of exocytosis in the RBL-2H3 mast cell line. Blank, U., Cyprien, B., Martin-Verdeaux, S., Paumet, F., Pombo, I., Rivera, J., Roa, M., Varin-Blank, N. Mol. Immunol. (2002) [Pubmed]
  6. Differential expression of SNAP-25 isoforms and SNAP-23 in the adrenal gland. Grant, N.J., Hepp, R., Krause, W., Aunis, D., Oehme, P., Langley, K. J. Neurochem. (1999) [Pubmed]
  7. Syntaxin 2 and SNAP-23 are required for regulated surfactant secretion. Abonyo, B.O., Gou, D., Wang, P., Narasaraju, T., Wang, Z., Liu, L. Biochemistry (2004) [Pubmed]
  8. Organization of the secretory machinery in the rodent brain: distribution of the t-SNAREs, SNAP-25 and SNAP-23. Chen, D., Minger, S.L., Honer, W.G., Whiteheart, S.W. Brain Res. (1999) [Pubmed]
  9. Effect of cholesterol depletion on exocytosis of alveolar type II cells. Chintagari, N.R., Jin, N., Wang, P., Narasaraju, T.A., Chen, J., Liu, L. Am. J. Respir. Cell Mol. Biol. (2006) [Pubmed]
  10. Interaction of SNARE proteins in rat parotid acinar cells. Takuma, T., Arakawa, T., Tajima, Y. Arch. Oral Biol. (2000) [Pubmed]
  11. Munc18-2/syntaxin3 complexes are spatially separated from syntaxin3-containing SNARE complexes. Pombo, I., Rivera, J., Blank, U. FEBS Lett. (2003) [Pubmed]
  12. 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]
  13. Evaluation of toxicological monitoring markers using proteomic analysis in rats exposed to formaldehyde. Im, H., Oh, E., Mun, J., Khim, J.Y., Lee, E., Kang, H.S., Kim, E., Kim, H., Won, N.H., Kim, Y.H., Jung, W.W., Sul, D. J. Proteome Res. (2006) [Pubmed]
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