VAMP2

Vesicle-associated membrane protein 2 (VAMP2) is a protein that in humans is encoded by the VAMP2 gene.[5][6]

VAMP2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesVAMP2, SYB2, VAMP-2, vesicle associated membrane protein 2, NEDHAHM
External IDsOMIM: 185881 MGI: 1313277 HomoloGene: 7591 GeneCards: VAMP2
Orthologs
SpeciesHumanMouse
Entrez

6844

22318

Ensembl

ENSG00000220205

ENSMUSG00000020894

UniProt

P63027

P63044

RefSeq (mRNA)

NM_014232
NM_001330125

NM_009497

RefSeq (protein)

NP_001317054
NP_055047

NP_033523

Location (UCSC)Chr 17: 8.16 – 8.16 MbChr 11: 68.98 – 68.98 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
Hypothetic models of VAMP2 conformations and engagement in SNARE complex assembly for neurotransmitter release

Function

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 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.[7] The protein forms a stable complex with syntaxin, synaptosomal-associated protein, 25 kD, and complexin. It also forms a distinct complex with synaptophysin.[6]

Clinical significance

Heterozygous mutations in VAMP2 cause a neurodevelopmental disorder with hypotonia and autistic features (with or without hyperkinetic movements).[8][9][10]

Interactions

VAMP2 has been shown to interact with:

References
  1. GRCh38: Ensembl release 89: ENSG00000220205 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000020894 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Archer BT, Ozçelik T, Jahn R, Francke U, Südhof TC (Oct 1990). "Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2". The Journal of Biological Chemistry. 265 (28): 17267–73. doi:10.1016/S0021-9258(17)44898-8. PMID 1976629.
  6. "Entrez Gene: VAMP2 vesicle-associated membrane protein 2 (synaptobrevin 2)".
  7. 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. Bibcode:2001Sci...294.1117S. doi:10.1126/science.1064335. PMID 11691998. S2CID 40321111.
  8. Salpietro V, Malintan NT, Llano-Rivas I, et al. (Apr 2019). "Mutations in the Neuronal Vesicular SNARE VAMP2 Affect Synaptic Membrane Fusion and Impair Human Neurodevelopment". The American Journal of Human Genetics. 104 (4): 721‐730. doi:10.1016/j.ajhg.2019.02.016. PMC 6451933. PMID 30929742.
  9. Sunaga Y, Muramatsu K, Kosaki K, et al. (Apr 2020). "Variant in the neuronal vesicular SNARE VAMP2 (synaptobrevin-2): First report in Japan". Brain and Development. 42 (7): 529–533. doi:10.1016/j.braindev.2020.04.001. PMID 32336483. S2CID 216095891.
  10. "OMIM entry: Neurodevelopmental disorder with hypotonia and autistic features with or without hyperkinetic movements".
  11. Martincic I, Peralta ME, Ngsee JK (Oct 1997). "Isolation and characterization of a dual prenylated Rab and VAMP2 receptor". The Journal of Biological Chemistry. 272 (43): 26991–8. doi:10.1074/jbc.272.43.26991. PMID 9341137.
  12. Li Y, Chin LS, Weigel C, Li L (Nov 2001). "Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis". The Journal of Biological Chemistry. 276 (44): 40824–33. doi:10.1074/jbc.M106141200. PMID 11524423.
  13. Hao JC, Salem N, Peng XR, Kelly RB, Bennett MK (Mar 1997). "Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes". The Journal of Neuroscience. 17 (5): 1596–603. doi:10.1523/JNEUROSCI.17-05-01596.1997. PMC 6573372. PMID 9030619.
  14. Chen X, Tomchick DR, Kovrigin E, Araç D, Machius M, Südhof TC, Rizo J (Jan 2002). "Three-dimensional structure of the complexin/SNARE complex". Neuron. 33 (3): 397–409. doi:10.1016/s0896-6273(02)00583-4. PMID 11832227. S2CID 17878965.
  15. 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". Journal of Immunology. 164 (11): 5850–7. doi:10.4049/jimmunol.164.11.5850. PMID 10820264.
  16. Imai A, Nashida T, Yoshie S, Shimomura H (Aug 2003). "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Archives of Oral Biology. 48 (8): 597–604. doi:10.1016/s0003-9969(03)00116-x. PMID 12828989.
  17. 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". The Journal of Biological Chemistry. 275 (11): 8240–7. doi:10.1074/jbc.275.11.8240. PMID 10713150.
  18. Dulubova I, Sugita S, Hill S, Hosaka M, Fernandez I, Südhof TC, Rizo J (Aug 1999). "A conformational switch in syntaxin during exocytosis: role of munc18". The EMBO Journal. 18 (16): 4372–82. doi:10.1093/emboj/18.16.4372. PMC 1171512. PMID 10449403.
  19. McMahon HT, Missler M, Li C, Südhof TC (Oct 1995). "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell. 83 (1): 111–9. doi:10.1016/0092-8674(95)90239-2. PMID 7553862. S2CID 675343.
  20. Pérez-Brangulí F, Muhaisen A, Blasi J (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". Molecular and Cellular Neurosciences. 20 (2): 169–80. doi:10.1006/mcne.2002.1122. PMID 12093152. S2CID 23927545.
  21. Margittai M, Otto H, Jahn R (Mar 1999). "A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains". FEBS Letters. 446 (1): 40–4. doi:10.1016/s0014-5793(99)00028-9. PMID 10100611. S2CID 9115709.
  22. Mollinedo F, Martín-Martín B, Calafat J, Nabokina SM, Lazo PA (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". Journal of Immunology. 170 (2): 1034–42. doi:10.4049/jimmunol.170.2.1034. PMID 12517971.
  23. Jagadish MN, Fernandez CS, Hewish DR, Macaulay SL, Gough KH, Grusovin J, Verkuylen A, Cosgrove L, Alafaci A, Frenkel MJ, Ward CW (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". The Biochemical Journal. 317. 317 (3): 945–54. doi:10.1042/bj3170945. PMC 1217577. PMID 8760387.
  24. Reed GL, Houng AK, Fitzgerald ML (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. 93 (8): 2617–26. doi:10.1182/blood.V93.8.2617. PMID 10194441.

Further reading
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