SNAP25

Abbozzo proteine
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SNAP25
Gene
Entrez6616
LocusChr. 20 p
Proteina
OMIM600322
PDB1jth
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La proteina sinaptosomale associata 25 (SNAP25) è una proteina SNARE con peso molecolare di 25 kilodalton (kDa), che nell'uomo è codificata dal gene SNAP25. Fa parte del Sinaptosoma, ovvero della struttura deputata al rilascio di Acetilcolina da parte della membrana del Motoneurone inferiore. È bloccata selettivamente dai tipi A C ed F della Neurotossina Botulinica.

Bibliografia

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  • Hanson PI, Otto H, Barton N, Jahn R, The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin, in J. Biol. Chem., vol. 270, n. 28, 1995, pp. 16955–61, DOI:10.1074/jbc.270.28.16955, PMID 7622514.
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  • Ravichandran V, Chawla A, Roche PA, Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues, in J. Biol. Chem., vol. 271, n. 23, 1996, pp. 13300–3, DOI:10.1074/jbc.271.23.13300, PMID 8663154.
  • Rettig J, Sheng ZH, Kim DK, et al., Isoform-specific interaction of the alpha1A subunits of brain Ca2+ channels with the presynaptic proteins syntaxin and SNAP-25, in Proc. Natl. Acad. Sci. U.S.A., vol. 93, n. 14, 1996, pp. 7363–8, DOI:10.1073/pnas.93.14.7363, PMC 38990, PMID 8692999.
  • Jagadish MN, Fernandez CS, Hewish DR, et al., Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2, in Biochem. J., 317 ( Pt 3), 1996, pp. 945–54, PMC 1217577, PMID 8760387.
  • Betz A, Okamoto M, Benseler F, Brose N, Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin, in J. Biol. Chem., vol. 272, n. 4, 1997, pp. 2520–6, DOI:10.1074/jbc.272.4.2520, PMID 8999968.
  • Araki S, Tamori Y, Kawanishi M, et al., Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c, in Biochem. Biophys. Res. Commun., vol. 234, n. 1, 1997, pp. 257–62, DOI:10.1006/bbrc.1997.6560, PMID 9168999.
  • Lane SR, Liu Y, Characterization of the palmitoylation domain of SNAP-25, in J. Neurochem., vol. 69, n. 5, 1997, pp. 1864–9, DOI:10.1046/j.1471-4159.1997.69051864.x, PMID 9349529.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al., Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library, in Gene, vol. 200, n. 1-2, 1997, pp. 149–56, DOI:10.1016/S0378-1119(97)00411-3, PMID 9373149.
  • Okamoto M, Südhof TC, Mints, Munc18-interacting proteins in synaptic vesicle exocytosis, in J. Biol. Chem., vol. 272, n. 50, 1998, pp. 31459–64, DOI:10.1074/jbc.272.50.31459, PMID 9395480.
  • Low SH, Roche PA, Anderson HA, et al., Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells, in J. Biol. Chem., vol. 273, n. 6, 1998, pp. 3422–30, DOI:10.1074/jbc.273.6.3422, PMID 9452464.
  • Poirier MA, Hao JC, Malkus PN, et al., Protease resistance of syntaxin.SNAP-25.VAMP complexes. Implications for assembly and structure, in J. Biol. Chem., vol. 273, n. 18, 1998, pp. 11370–7, DOI:10.1074/jbc.273.18.11370, PMID 9556632.
  • Prekeris R, Klumperman J, Chen YA, Scheller RH, Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes, in J. Cell Biol., vol. 143, n. 4, 1998, pp. 957–71, DOI:10.1083/jcb.143.4.957, PMC 2132958, PMID 9817754.
  • Gonelle-Gispert C, Halban PA, Niemann H, et al., SNAP-25a and -25b isoforms are both expressed in insulin-secreting cells and can function in insulin secretion, in Biochem. J., 339 ( Pt 1), 1999, pp. 159–65, DOI:10.1042/0264-6021:3390159, PMC 1220140, PMID 10085240.
  • Ilardi JM, Mochida S, Sheng ZH, Snapin: a SNARE-associated protein implicated in synaptic transmission, in Nat. Neurosci., vol. 2, n. 2, 1999, pp. 119–24, DOI:10.1038/5673, PMID 10195194.
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