VAMP1 explained

Vesicle-associated membrane protein 1 (VAMP1) is a protein that in humans is encoded by the VAMP1 gene.^{[1] [2]}

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. VAMP1 is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Multiple alternative splice variants that encode proteins with alternative carboxy ends have been described, but the full-length nature of some variants has not been defined.

Clinical significance

Homozygous mutations in VAMP1 have been identified in a series of children affected with a form of congenital myasthenic syndrome and similar presynaptic features in these patients and the knock-out VAMP1 mouse have been demonstrated.^[3]

VAMP1 expression has been linked to higher survival rates for lung cancer patients.^[4]

Further reading

• Ravichandran V, Chawla A, Roche PA . Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues . The Journal of Biological Chemistry . 271 . 23 . 13300–3 . June 1996 . 8663154 . 10.1074/jbc.271.23.13300 . free .
• Jagadish MN, Fernandez CS, Hewish DR, Macaulay SL, Gough KH, Grusovin J, Verkuylen A, Cosgrove L, Alafaci A, Frenkel MJ, Ward CW . 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 (Pt 3) . 3. 945–54 . August 1996 . 8760387 . 1217577 . 10.1042/bj3170945 . 317 .
• 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 .
• Weir ML, Klip A, Trimble WS . 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 . The Biochemical Journal . 333 (Pt 2) . 2. 247–51 . July 1998 . 9657962 . 1219579 . 10.1042/bj3330247 . 333 .
• Isenmann S, Khew-Goodall Y, Gamble J, Vadas M, Wattenberg BW . A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal . Molecular Biology of the Cell . 9 . 7 . 1649–60 . July 1998 . 9658161 . 25402 . 10.1091/mbc.9.7.1649 .
• Nishimura Y, Hayashi M, Inada H, Tanaka T . Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins . Biochemical and Biophysical Research Communications . 254 . 1 . 21–6 . January 1999 . 9920726 . 10.1006/bbrc.1998.9876 .
• Berglund L, Hoffmann HJ, Dahl R, Petersen TE . VAMP-1 has a highly variable C-terminus generated by alternative splicing . Biochemical and Biophysical Research Communications . 264 . 3 . 777–80 . November 1999 . 10544008 . 10.1006/bbrc.1999.1588 .
• Pérez-Brangulí F, Muhaisen A, Blasi J . 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 . June 2002 . 12093152 . 10.1006/mcne.2002.1122 . 23927545 .
• Imabayashi H, Mori T, Gojo S, Kiyono T, Sugiyama T, Irie R, Isogai T, Hata J, Toyama Y, Umezawa A . Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis . Experimental Cell Research . 288 . 1 . 35–50 . August 2003 . 12878157 . 10.1016/S0014-4827(03)00130-7 .
• Huda Zoghbi . 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 . 2005Natur.437.1173R . 4427026 .

Notes and References

1. Archer BT, Ozçelik T, Jahn R, Francke U, Südhof TC . Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2 . The Journal of Biological Chemistry . 265 . 28 . 17267–73 . October 1990 . 10.1016/S0021-9258(17)44898-8 . 1976629 . free .
2. Web site: Entrez Gene: VAMP1 vesicle-associated membrane protein 1 (synaptobrevin 1).
3. Salpietro V, Lin W, Delle Vedove A, Storbeck M, Liu Y, Efthymiou S, Manole A, Wiethoff S, Ye Q, Saggar A, McElreavey K, Krishnakumar SS, Pitt M, Bello OD, Rothman JE, Basel-Vanagaite L, Hubshman MW, Aharoni S, Manzur AY, Wirth B, Houlden H . Homozygous mutations in VAMP1 cause a presynaptic congenital myasthenic syndrome . Annals of Neurology . 81 . 4 . 597–603 . April 2017 . 28253535 . 5413866 . 10.1002/ana.24905 .
4. Web site: Research update from the MCM team (March 2023). World Community Grid. 20 March 2023. 21 May 2024.