VAMP3 explained

Vesicle-associated membrane protein 3 is a protein that in humans is encoded by the VAMP3 gene.[1] [2]

Function

Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. This gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Because of its high homology to other known VAMPs, its broad tissue distribution, and its subcellular localization, the protein encoded by this gene was shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.

Interactions

VAMP3 has been shown to interact with

Further reading

Notes and References

  1. Bernstein AM, Whiteheart SW . Identification of a cellubrevin/vesicle associated membrane protein 3 homologue in human platelets . Blood . 93 . 2 . 571–9 . January 1999 . 9885218 . 10.1182/blood.V93.2.571.
  2. Web site: Entrez Gene: VAMP3 vesicle-associated membrane protein 3 (cellubrevin).
  3. Annaert WG, Becker B, Kistner U, Reth M, Jahn R . Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31 . The Journal of Cell Biology . 139 . 6 . 1397–410 . December 1997 . 9396746 . 2132629 . 10.1083/jcb.139.6.1397 .
  4. Hager HA, Roberts RJ, Cross EE, Proux-Gillardeaux V, Bader DM . Identification of a novel Bves function: regulation of vesicular transport . The EMBO Journal . 29 . 3 . 532–45 . February 2010 . 20057356 . 2830705 . 10.1038/emboj.2009.379 .
  5. Freedman SJ, Song HK, Xu Y, Sun ZY, Eck MJ . Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain . The Journal of Biological Chemistry . 278 . 15 . 13462–7 . April 2003 . 12556468 . 10.1074/jbc.M210483200 . free .
  6. Imai A, Nashida T, Yoshie S, Shimomura H . 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 . August 2003 . 12828989 . 10.1016/S0003-9969(03)00116-X .
  7. Paumet F, Le Mao J, Martin S, Galli T, David B, Blank U, Roa M . 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 . June 2000 . 10820264 . 10.4049/jimmunol.164.11.5850 . free .
  8. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M . Towards a proteome-scale map of the human protein-protein interaction network . Nature . 437 . 7062 . 1173–8 . October 2005 . 16189514 . 10.1038/nature04209 . Huda Zoghbi . 2005Natur.437.1173R . 4427026 .
  9. Polgár J, Chung SH, Reed GL . Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion . Blood . 100 . 3 . 1081–3 . August 2002 . 12130530 . 10.1182/blood.V100.3.1081 . 36597939 .
  10. Mallard F, Tang BL, Galli T, Tenza D, Saint-Pol A, Yue X, Antony C, Hong W, Goud B, Johannes L . Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform . The Journal of Cell Biology . 156 . 4 . 653–64 . February 2002 . 11839770 . 2174079 . 10.1083/jcb.200110081 .