VAMP2

Vesicle-associated membrane protein 2 (synaptobrevin 2)
	; PDB rendering based on 1kil.
Available structures
PDB	3FIE, 3FII
Identifiers
Symbols	VAMP2; FLJ11460; SYB2; VAMP-2
External IDs	OMIM: 185881 MGI: 1313277 HomoloGene: 7591 GeneCards: VAMP2 Gene
Gene Ontology
Molecular function	• protein binding; • calmodulin binding; • phospholipid binding; • syntaxin binding;
Cellular component	• trans-Golgi network; • plasma membrane; • plasma membrane; • integral to plasma membrane; • synaptosome; • cell junction; • clathrin-coated vesicle; • endocytic vesicle membrane; • secretory granule membrane; • synaptic vesicle membrane; • cytoplasmic vesicle; • zymogen granule membrane; • synapse; • perinuclear region of cytoplasm; • clathrin sculpted glutamate transport vesicle membrane; • clathrin sculpted glutamate transport vesicle membrane; • clathrin sculpted gamma-aminobutyric acid transport vesicle membrane; • clathrin sculpted gamma-aminobutyric acid transport vesicle membrane; • clathrin sculpted monoamine transport vesicle membrane;
Biological process	• energy reserve metabolic process; • post-Golgi vesicle-mediated transport; • cellular membrane fusion; • synaptic transmission; • neurotransmitter secretion; • glutamate secretion; • cellular membrane organization; • synaptic vesicle exocytosis; • vesicle-mediated transport; • calcium ion-dependent exocytosis; • regulation of exocytosis; • regulation of insulin secretion;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs

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Vesicle-associated membrane protein 2 is a protein that in humans is encoded by the VAMP2 gene.^[1]^[2]

Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP2 is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. VAMP2 is a likely candidate gene for familial infantile myasthenia (FIMG) because of its map location and because it encodes a synaptic vesicle protein of the type that has been implicated in the pathogenesis of FIMG. VAMP2 is thought to participate in neurotransmitter release at a step between docking and fusion. Mice lacking functional synaptobrevin2/VAMP2 gene cannot survive after birth, and have a dramatically reduced synaptic transmission, around 10% of control.^[3] The protein forms a stable complex with syntaxin, synaptosomal-associated protein, 25 kD, and complexin. It also forms a distinct complex with synaptophysin.^[2]

[edit] Interactions

VAMP2 has been shown to interact with STX4,^[4]^[5]^[6]^[7] SNAP-25,^[8]^[9]^[10] SNAP23,^[4]^[11]^[12] STX1A^[9]^[10]^[13]^[14]^[15]^[16] and RABAC1.^[17]

[edit] References

^ Archer BT 3rd, Ozcelik T, Jahn R, Francke U, Sudhof TC (Nov 1990). "Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2". J Biol Chem 265 (28): 17267–73. PMID 1976629.
^ ^a ^b "Entrez Gene: VAMP2 vesicle-associated membrane protein 2 (synaptobrevin 2)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6844.
^ Schoch S, Deák F, Königstorfer A, Mozhayeva M, Sara Y, Südhof TC, Kavalali ET. (Nov 2001). "SNARE function analyzed in synaptobrevin/VAMP knockout mice". Science 294 (5544): 1117–22. doi:10.1126/science.1064335. PMID 11691998.
^ ^a ^b Paumet, F; Le Mao J, Martin S, Galli T, David B, Blank U, Roa M (Jun. 2000). "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". J. Immunol. (UNITED STATES) 164 (11): 5850–7. ISSN 0022-1767. PMID 10820264.
^ Mollinedo, Faustino; Martín-Martín Belén, Calafat Jero, Nabokina Svetlana M, Lazo Pedro A (Jan. 2003). "Role of vesicle-associated membrane protein-2, through Q-soluble N-ethylmaleimide-sensitive factor attachment protein receptor/R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor interaction, in the exocytosis of specific and tertiary granules of human neutrophils". J. Immunol. (United States) 170 (2): 1034–42. ISSN 0022-1767. PMID 12517971.
^ Jagadish, M N; Fernandez C S, Hewish D R, Macaulay S L, Gough K H, Grusovin J, Verkuylen A, Cosgrove L, Alafaci A, Frenkel M J, Ward C W (Aug. 1996). "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". Biochem. J.. 317 (ENGLAND) ( Pt 3): 945–54. ISSN 0264-6021. PMC 1217577. PMID 8760387. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1217577.
^ Reed, G L; Houng A K, Fitzgerald M L (Apr. 1999). "Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: implications for platelet secretion". Blood (UNITED STATES) 93 (8): 2617–26. ISSN 0006-4971. PMID 10194441.
^ Li, Y; Chin L S, Weigel C, Li L (Nov. 2001). "Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis". J. Biol. Chem. (United States) 276 (44): 40824–33. doi:10.1074/jbc.M106141200. ISSN 0021-9258. PMID 11524423.
^ ^a ^b Hao, J C; Salem N, Peng X R, Kelly R B, Bennett M K (Mar. 1997). "Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes". J. Neurosci. (UNITED STATES) 17 (5): 1596–603. ISSN 0270-6474. PMID 9030619.
^ ^a ^b Chen, Xiaocheng; Tomchick Diana R, Kovrigin Evguenii, Araç Demet, Machius Mischa, Südhof Thomas C, Rizo Josep (Jan. 2002). "Three-dimensional structure of the complexin/SNARE complex". Neuron (United States) 33 (3): 397–409. doi:10.1016/S0896-6273(02)00583-4. ISSN 0896-6273. PMID 11832227.
^ Imai, Akane; Nashida Tomoko, Yoshie Sumio, Shimomura Hiromi (Aug. 2003). "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Arch. Oral Biol. (England) 48 (8): 597–604. doi:10.1016/S0003-9969(03)00116-X. ISSN 0003-9969. PMID 12828989.
^ Kawanishi, M; Tamori Y, Okazawa H, Araki S, Shinoda H, Kasuga M (Mar. 2000). "Role of SNAP23 in insulin-induced translocation of GLUT4 in 3T3-L1 adipocytes. Mediation of complex formation between syntaxin4 and VAMP2". J. Biol. Chem. (UNITED STATES) 275 (11): 8240–7. doi:10.1074/jbc.275.11.8240. ISSN 0021-9258. PMID 10713150.
^ Dulubova, I; Sugita S, Hill S, Hosaka M, Fernandez I, Südhof T C, Rizo J (Aug. 1999). "A conformational switch in syntaxin during exocytosis: role of munc18". EMBO J. (ENGLAND) 18 (16): 4372–82. doi:10.1093/emboj/18.16.4372. ISSN 0261-4189. PMC 1171512. PMID 10449403. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171512.
^ McMahon, H T; Missler M, Li C, Südhof T C (Oct. 1995). "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell (UNITED STATES) 83 (1): 111–9. doi:10.1016/0092-8674(95)90239-2. ISSN 0092-8674. PMID 7553862.
^ Pérez-Brangulí, Francesc; Muhaisen Ashraf, Blasi Juan (Jun. 2002). "Munc 18a binding to syntaxin 1A and 1B isoforms defines its localization at the plasma membrane and blocks SNARE assembly in a three-hybrid system assay". Mol. Cell. Neurosci. (United States) 20 (2): 169–80. doi:10.1006/mcne.2002.1122. ISSN 1044-7431. PMID 12093152.
^ Margittai, M; Otto H, Jahn R (Mar. 1999). "A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains". FEBS Lett. (NETHERLANDS) 446 (1): 40–4. doi:10.1016/S0014-5793(99)00028-9. ISSN 0014-5793. PMID 10100611.
^ Martincic, I; Peralta M E, Ngsee J K (Oct. 1997). "Isolation and characterization of a dual prenylated Rab and VAMP2 receptor". J. Biol. Chem. (UNITED STATES) 272 (43): 26991–8. doi:10.1074/jbc.272.43.26991. ISSN 0021-9258. PMID 9341137.

[edit] Further reading

Brumell JH, Volchuk A, Sengelov H, et al. (1996). "Subcellular distribution of docking/fusion proteins in neutrophils, secretory cells with multiple exocytic compartments.". J. Immunol. 155 (12): 5750–9. PMID 7499863.
Kutay U, Ahnert-Hilger G, Hartmann E, et al. (1995). "Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane.". EMBO J. 14 (2): 217–23. PMC 398073. PMID 7835332. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=398073.
Chapman ER, An S, Barton N, Jahn R (1994). "SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils.". J. Biol. Chem. 269 (44): 27427–32. PMID 7961655.
Hunt JM, Bommert K, Charlton MP, et al. (1994). "A post-docking role for synaptobrevin in synaptic vesicle fusion.". Neuron 12 (6): 1269–79. doi:10.1016/0896-6273(94)90443-X. PMID 8011337.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Jagadish MN, Fernandez CS, Hewish DR, et al. (1996). "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.". Biochem. J.. 317 ( Pt 3): 945–54. PMC 1217577. PMID 8760387. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1217577.
Mandon B, Chou CL, Nielsen S, Knepper MA (1996). "Syntaxin-4 is localized to the apical plasma membrane of rat renal collecting duct cells: possible role in aquaporin-2 trafficking.". J. Clin. Invest. 98 (4): 906–13. doi:10.1172/JCI118873. PMC 507504. PMID 8770861. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=507504.
Timmers KI, Clark AE, Omatsu-Kanbe M, et al. (1997). "Identification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion protein.". Biochem. J.. 320 ( Pt 2): 429–36. PMC 1217948. PMID 8973549. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1217948.
Betz A, Okamoto M, Benseler F, Brose N (1997). "Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin.". J. Biol. Chem. 272 (4): 2520–6. doi:10.1074/jbc.272.4.2520. PMID 8999968.
Hao JC, Salem N, Peng XR, et al. (1997). "Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes.". J. Neurosci. 17 (5): 1596–603. PMID 9030619.
Martincic I, Peralta ME, Ngsee JK (1997). "Isolation and characterization of a dual prenylated Rab and VAMP2 receptor.". J. Biol. Chem. 272 (43): 26991–8. doi:10.1074/jbc.272.43.26991. PMID 9341137.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Weir ML, Klip A, Trimble WS (1998). "Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a broadly expressed protein that binds to VAMP.". Biochem. J.. 333 ( Pt 2): 247–51. PMC 1219579. PMID 9657962. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1219579.
Isenmann S, Khew-Goodall Y, Gamble J, et al. (1999). "A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal.". Mol. Biol. Cell 9 (7): 1649–60. PMC 25402. PMID 9658161. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=25402.
Prekeris R, Klumperman J, Chen YA, Scheller RH (1998). "Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes.". J. Cell Biol. 143 (4): 957–71. doi:10.1083/jcb.143.4.957. PMC 2132958. PMID 9817754. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2132958.
Nishimura Y, Hayashi M, Inada H, Tanaka T (1999). "Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins.". Biochem. Biophys. Res. Commun. 254 (1): 21–6. doi:10.1006/bbrc.1998.9876. PMID 9920726.
Valdez AC, Cabaniols JP, Brown MJ, Roche PA (1999). "Syntaxin 11 is associated with SNAP-23 on late endosomes and the trans-Golgi network.". J. Cell. Sci.. 112 ( Pt 6): 845–54. PMID 10036234.
Margittai M, Otto H, Jahn R (1999). "A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains.". FEBS Lett. 446 (1): 40–4. doi:10.1016/S0014-5793(99)00028-9. PMID 10100611.
Fasshauer D, Antonin W, Margittai M, et al. (1999). "Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties.". J. Biol. Chem. 274 (22): 15440–6. doi:10.1074/jbc.274.22.15440. PMID 10336434.

[pmid1976629-0] Archer BT 3rd, Ozcelik T, Jahn R, Francke U, Sudhof TC (Nov 1990). "Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2". J Biol Chem 265 (28): 17267–73. PMID 1976629.

[entrez-1] "Entrez Gene: VAMP2 vesicle-associated membrane protein 2 (synaptobrevin 2)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6844.

[pmid11691998-2] Schoch S, Deák F, Königstorfer A, Mozhayeva M, Sara Y, Südhof TC, Kavalali ET. (Nov 2001). "SNARE function analyzed in synaptobrevin/VAMP knockout mice". Science 294 (5544): 1117–22. doi:10.1126/science.1064335. PMID 11691998.

[pmid10820264-3] Paumet, F; Le Mao J, Martin S, Galli T, David B, Blank U, Roa M (Jun. 2000). "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". J. Immunol. (UNITED STATES) 164 (11): 5850–7. ISSN 0022-1767. PMID 10820264.

[pmid12517971-4] Mollinedo, Faustino; Martín-Martín Belén, Calafat Jero, Nabokina Svetlana M, Lazo Pedro A (Jan. 2003). "Role of vesicle-associated membrane protein-2, through Q-soluble N-ethylmaleimide-sensitive factor attachment protein receptor/R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor interaction, in the exocytosis of specific and tertiary granules of human neutrophils". J. Immunol. (United States) 170 (2): 1034–42. ISSN 0022-1767. PMID 12517971.

[pmid8760387-5] Jagadish, M N; Fernandez C S, Hewish D R, Macaulay S L, Gough K H, Grusovin J, Verkuylen A, Cosgrove L, Alafaci A, Frenkel M J, Ward C W (Aug. 1996). "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". Biochem. J.. 317 (ENGLAND) ( Pt 3): 945–54. ISSN 0264-6021. PMC 1217577. PMID 8760387. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1217577.

[pmid10194441-6] Reed, G L; Houng A K, Fitzgerald M L (Apr. 1999). "Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: implications for platelet secretion". Blood (UNITED STATES) 93 (8): 2617–26. ISSN 0006-4971. PMID 10194441.

[pmid11524423-7] Li, Y; Chin L S, Weigel C, Li L (Nov. 2001). "Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis". J. Biol. Chem. (United States) 276 (44): 40824–33. doi:10.1074/jbc.M106141200. ISSN 0021-9258. PMID 11524423.

[pmid9030619-8] Hao, J C; Salem N, Peng X R, Kelly R B, Bennett M K (Mar. 1997). "Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes". J. Neurosci. (UNITED STATES) 17 (5): 1596–603. ISSN 0270-6474. PMID 9030619.

[pmid11832227-9] Chen, Xiaocheng; Tomchick Diana R, Kovrigin Evguenii, Araç Demet, Machius Mischa, Südhof Thomas C, Rizo Josep (Jan. 2002). "Three-dimensional structure of the complexin/SNARE complex". Neuron (United States) 33 (3): 397–409. doi:10.1016/S0896-6273(02)00583-4. ISSN 0896-6273. PMID 11832227.

[pmid12828989-10] Imai, Akane; Nashida Tomoko, Yoshie Sumio, Shimomura Hiromi (Aug. 2003). "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Arch. Oral Biol. (England) 48 (8): 597–604. doi:10.1016/S0003-9969(03)00116-X. ISSN 0003-9969. PMID 12828989.

[pmid10713150-11] Kawanishi, M; Tamori Y, Okazawa H, Araki S, Shinoda H, Kasuga M (Mar. 2000). "Role of SNAP23 in insulin-induced translocation of GLUT4 in 3T3-L1 adipocytes. Mediation of complex formation between syntaxin4 and VAMP2". J. Biol. Chem. (UNITED STATES) 275 (11): 8240–7. doi:10.1074/jbc.275.11.8240. ISSN 0021-9258. PMID 10713150.

[pmid10449403-12] Dulubova, I; Sugita S, Hill S, Hosaka M, Fernandez I, Südhof T C, Rizo J (Aug. 1999). "A conformational switch in syntaxin during exocytosis: role of munc18". EMBO J. (ENGLAND) 18 (16): 4372–82. doi:10.1093/emboj/18.16.4372. ISSN 0261-4189. PMC 1171512. PMID 10449403. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171512.

[pmid7553862-13] McMahon, H T; Missler M, Li C, Südhof T C (Oct. 1995). "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell (UNITED STATES) 83 (1): 111–9. doi:10.1016/0092-8674(95)90239-2. ISSN 0092-8674. PMID 7553862.

[pmid12093152-14] Pérez-Brangulí, Francesc; Muhaisen Ashraf, Blasi Juan (Jun. 2002). "Munc 18a binding to syntaxin 1A and 1B isoforms defines its localization at the plasma membrane and blocks SNARE assembly in a three-hybrid system assay". Mol. Cell. Neurosci. (United States) 20 (2): 169–80. doi:10.1006/mcne.2002.1122. ISSN 1044-7431. PMID 12093152.

[pmid10100611-15] Margittai, M; Otto H, Jahn R (Mar. 1999). "A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains". FEBS Lett. (NETHERLANDS) 446 (1): 40–4. doi:10.1016/S0014-5793(99)00028-9. ISSN 0014-5793. PMID 10100611.

[pmid9341137-16] Martincic, I; Peralta M E, Ngsee J K (Oct. 1997). "Isolation and characterization of a dual prenylated Rab and VAMP2 receptor". J. Biol. Chem. (UNITED STATES) 272 (43): 26991–8. doi:10.1074/jbc.272.43.26991. ISSN 0021-9258. PMID 9341137.

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VAMP2

[edit] Interactions

[edit] References

[edit] Further reading

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