VAMP2

From Wikipedia, the free encyclopedia

Vesicle-associated membrane protein 2 (synaptobrevin 2)

PDB rendering based on 1kil.

Available structures: 1kil, 1n7s, 1sfc

Identifiers

Symbol(s)

VAMP2; FLJ11460; SYB2; VAMP-2

External IDs

OMIM: 185881 MGI: 1313277 HomoloGene: 7591

Gene ontology
Molecular Function:	• SNARE binding • calmodulin binding • phospholipid binding
Cellular Component:	• integral to plasma membrane • membrane • synaptosome • secretory granule • synaptic vesicle membrane • zymogen granule membrane • synapse
Biological Process:	• membrane fusion • synaptic vesicle exocytosis • vesicle-mediated transport • calcium ion-dependent exocytosis • regulation of exocytosis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_014232 (mRNA)
NP_055047 (protein)

NM_009497 (mRNA)
NP_033523 (protein)

Location

Chr 17: 8 - 8.01 Mb

Chr 11: 68.9 - 68.91 Mb

Pubmed search

[1]

[2]

Vesicle-associated membrane protein 2 (synaptobrevin 2), also known as VAMP2, is a human gene.^[1]

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. The protein forms a stable complex with syntaxin, synaptosomal-associated protein, 25 kD, and synaptotagmin. It also forms a distinct complex with synaptophysin.^[1]

[edit] References

^ ^a ^b Entrez Gene: VAMP2 vesicle-associated membrane protein 2 (synaptobrevin 2).

[edit] Further reading

Archer BT, Ozçelik T, Jahn R, et al. (1990). "Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2.". J. Biol. Chem. 265 (28): 17267–73. PMID 1976629.
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. PMID 7835332.
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. 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. 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. PMID 8760387.
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. PMID 8770861.
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. PMID 8973549.
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. 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. 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. 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. PMID 9657962.
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. PMID 9658161.
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. PMID 9817754.
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. 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. PMID 10336434.