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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/09/12 14:04:55」(JST)

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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]

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]

References

^ Archer BT 3rd, Ozcelik T, Jahn R, Francke U, Sudhof TC (November 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. (November 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 (June 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 (January 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 (August 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. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1217577/.
^ Reed, G L; Houng A K, Fitzgerald M L (April 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 (November 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 (March 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 (January 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 (August 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 (March 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 (August 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. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1171512/.
^ McMahon, H T; Missler M, Li C, Südhof T C (October 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 (June 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 (March 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 (October 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.

English Journal

A botulinum toxin-derived targeted secretion inhibitor downregulates the GH/IGF1 axis.

Somm E, Bonnet N, Martinez A, Marks PM, Cadd VA, Elliott M, Toulotte A, Ferrari SL, Rizzoli R, Hüppi PS, Harper E, Melmed S, Jones R, Aubert ML.AbstractBotulinum neurotoxins (BoNTs) are zinc endopeptidases that block release of the neurotransmitter acetylcholine in neuromuscular synapses through cleavage of soluble N-ethylmaleimide-sensitive fusion (NSF) attachment protein receptor (SNARE) proteins, which promote fusion of synaptic vesicles to the plasma membrane. We designed and tested a BoNT-derived targeted secretion inhibitor (TSI) targeting pituitary somatotroph cells to suppress growth hormone (GH) secretion and treat acromegaly. This recombinant protein, called SXN101742, contains a modified GH-releasing hormone (GHRH) domain and the endopeptidase domain of botulinum toxin serotype D (GHRH-LHN/D, where HN/D indicates endopeptidase and translocation domain type D). In vitro, SXN101742 targeted the GHRH receptor and depleted a SNARE protein involved in GH exocytosis, vesicle-associated membrane protein 2 (VAMP2). In vivo, administering SXN101742 to growing rats produced a dose-dependent inhibition of GH synthesis, storage, and secretion. Consequently, hepatic IGF1 production and resultant circulating IGF1 levels were reduced. Accordingly, body weight, body length, organ weight, and bone mass acquisition were all decreased, reflecting the biological impact of SXN101742 on the GH/IGF1 axis. An inactivating 2-amino acid substitution within the zinc coordination site of the endopeptidase domain completely abolished SXN101742 inhibitory actions on GH and IGF1. Thus, genetically reengineered BoNTs can be targeted to nonneural cells to selectively inhibit hormone secretion, representing a new approach to treating hormonal excess.
The Journal of clinical investigation.J Clin Invest.2012 Aug 1. pii: 63232. doi: 10.1172/JCI63232. [Epub ahead of print]
Botulinum neurotoxins (BoNTs) are zinc endopeptidases that block release of the neurotransmitter acetylcholine in neuromuscular synapses through cleavage of soluble N-ethylmaleimide-sensitive fusion (NSF) attachment protein receptor (SNARE) proteins, which promote fusion of synaptic vesicles to the
PMID 22850878

Molecular Basis for Specific Regulation of Neuronal Kinesin-3 Motors by Doublecortin Family Proteins.

Liu JS, Schubert CR, Fu X, Fourniol FJ, Jaiswal JK, Houdusse A, Stultz CM, Moores CA, Walsh CA.SourceCenter for Neuroscience Research, Children's National Medical Center, Washington, DC 20010, USA; Division of Genetics, Howard Hughes Medical Institute, Manton Center for Orphan Diseases, Children's Hospital Boston, and Department of Pediatrics and Department of Neurology, Harvard Medical School, Boston, MA 02115, USA.
Molecular cell.Mol Cell.2012 Aug 1. [Epub ahead of print]
Doublecortin (Dcx) defines a growing family of microtubule (MT)-associated proteins (MAPs) involved in neuronal migration and process outgrowth. We show that Dcx is essential for the function of Kif1a, a kinesin-3 motor protein that traffics synaptic vesicles. Neurons lacking Dcx and/or its structur
PMID 22857951

Japanese Journal

1型糖尿病の膵島関連自己抗体

三浦順之助,内潟安子,岩本安彦
東京女子医科大学雑誌 81(E2), E78-E84, 2011-03-31
1型糖尿病は、膵β細胞が破壊されることによりインスリンの絶対的欠乏が生じて発症する病型であるが、自己免疫機序が関与する1A型と、発症機序の明らかでない特発性の1B型に亜分類される。1A型糖尿病の診断には、Islet cell antigen (ICA)をはじめとして、インスリン自己抗体(insulin autoantibody : IAA)、抗Glutamic acid decarboxylase …
NAID 110008441448

Myosin IIA participates in docking of Glut4 storage vesicles with the plasma membrane in 3T3-L1 adipocytes

Chung Le Thi Kim,Hosaka Toshio,Harada Nagakatsu,Jambaldorj Bayasgalan,Fukunaga Keiko,Nishiwaki Yuka,Teshigawara Kiyoshi,Sakai Tohru,Nakaya Yutaka,Funaki Makoto
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 391(1), 995-999, 2010
NAID 80020846276

VAMP2 Marks Quiescent Satellite Cells and Myotubes, but not Activated Myoblasts

Tajika Yuki,Takahashi Maiko,Hino Mizuki,Murakami Tohru,Yorifuji Hiroshi
ACTA HISTOCHEMICA ET CYTOCHEMICA 43(4), 107-114, 2010
… We examined the expression and intracellular localization of vesicle-associated membrane protein 2 (VAMP2) during the differentiation of skeletal muscle cells by immunofluorescence microscopy. … In isolated single myofibers, VAMP2 was expressed in quiescent satellite cells, downregulated in proliferating myoblastic cells, and re-expressed with differentiation. …
NAID 130000299893

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★リンクテーブル★

リンク元	「synaptobrevin 2」「小胞結合膜タンパク質2」「vesicle-associated membrane protein 2」

「synaptobrevin 2」

Vesicle-associated membrane protein 2 (synaptobrevin 2)
	; PDB rendering based on 1kil.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	3FIE, 3FII, 3RK2, 3RK3, 3RL0
Identifiers
Symbols	VAMP2; 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; • integral to plasma membrane; • synaptosome; • cell junction; • clathrin-coated vesicle; • endocytic vesicle membrane; • secretory granule membrane; • synaptic vesicle membrane; • zymogen granule membrane; • perinuclear region of cytoplasm; • clathrin sculpted glutamate transport vesicle membrane; • clathrin sculpted gamma-aminobutyric acid transport vesicle membrane; • synaptobrevin 2-SNAP-25-syntaxin-1a complex; • 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; • calcium ion-dependent exocytosis; • regulation of exocytosis; • small molecule metabolic process; • regulation of insulin secretion;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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