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Gene Review

Vamp2  -  vesicle-associated membrane protein 2

Mus musculus

Synonyms: Syb-2, Syb2, Synaptobrevin-2, VAMP-2, Vesicle-associated membrane protein 2, ...
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Disease relevance of Vamp2


High impact information on Vamp2


Chemical compound and disease context of Vamp2

  • Finally, glutamate and AA were released solely from neurons as tetanus toxin did not cleave astrocytic synaptobrevin-2, nor was AA released from pure astrocyte cultures using the same stimuli that were effective in mixed cultures [7].

Biological context of Vamp2


Anatomical context of Vamp2


Associations of Vamp2 with chemical compounds


Physical interactions of Vamp2

  • Together, these data suggest that Munc18c inhibits the docking/fusion of GLUT4-containing vesicles by blocking the binding of VAMP2 to syntaxin 4 [18].

Regulatory relationships of Vamp2


Other interactions of Vamp2

  • VAMP-1, VAMP-2, and cellubrevin cDNAs were isolated from a 3T3-L1 adipocyte expression library [6].
  • These data taken together strongly suggest a role for VAMP 2 in GLUT4 trafficking and also for syntaxin 4 [20].
  • Cleavage of SNAP-25 and VAMP-2 impairs store-operated Ca2+ entry in mouse pancreatic acinar cells [13].
  • Our results show that GLUT4 overexpression or deficiency affects the amount of other GLUT4-vesicle proteins including IRAP and VAMP2 and that GLUT4 sequestration is saturable [21].
  • In the current study, we used quantitative in situ hybridisation to examine mRNA expression of SNAREs (25 kDa synaptosome-associated protein (SNAP-25), syntaxin-1A and synaptobrevin-2) and SNARE-associated proteins (alpha-SNAP, CPLXI and CPLXII) in brain of R6/2 mice and their wild type littermates between 3 and 15 weeks of age [22].

Analytical, diagnostic and therapeutic context of Vamp2


  1. Cellubrevin is a resident protein of insulin-sensitive GLUT4 glucose transporter vesicles in 3T3-L1 adipocytes. Volchuk, A., Sargeant, R., Sumitani, S., Liu, Z., He, L., Klip, A. J. Biol. Chem. (1995) [Pubmed]
  2. Participation of syntaxin 1A in membrane trafficking involving neurite elongation and membrane expansion. Zhou, Q., Xiao, J., Liu, Y. J. Neurosci. Res. (2000) [Pubmed]
  3. SNARE function analyzed in synaptobrevin/VAMP knockout mice. Schoch, S., Deák, F., Königstorfer, A., Mozhayeva, M., Sara, Y., Südhof, T.C., Kavalali, E.T. Science (2001) [Pubmed]
  4. Rapid and reversible chemical inactivation of synaptic transmission in genetically targeted neurons. Karpova, A.Y., Tervo, D.G., Gray, N.W., Svoboda, K. Neuron (2005) [Pubmed]
  5. v-SNAREs control exocytosis of vesicles from priming to fusion. Borisovska, M., Zhao, Y., Tsytsyura, Y., Glyvuk, N., Takamori, S., Matti, U., Rettig, J., Südhof, T., Bruns, D. EMBO J. (2005) [Pubmed]
  6. The glucose transporter (GLUT-4) and vesicle-associated membrane protein-2 (VAMP-2) are segregated from recycling endosomes in insulin-sensitive cells. Martin, S., Tellam, J., Livingstone, C., Slot, J.W., Gould, G.W., James, D.E. J. Cell Biol. (1996) [Pubmed]
  7. Potassium-evoked glutamate release liberates arachidonic acid from cortical neurons. Taylor, A.L., Hewett, S.J. J. Biol. Chem. (2002) [Pubmed]
  8. Synaptobrevin is essential for fast synaptic-vesicle endocytosis. Deák, F., Schoch, S., Liu, X., Südhof, T.C., Kavalali, E.T. Nat. Cell Biol. (2004) [Pubmed]
  9. Binary interactions of the SNARE proteins syntaxin-4, SNAP23, and VAMP-2 and their regulation by phosphorylation. Foster, L.J., Yeung, B., Mohtashami, M., Ross, K., Trimble, W.S., Klip, A. Biochemistry (1998) [Pubmed]
  10. Genetic analysis of the rat hypodactylous mutation. Krenová, D., Jirsová, Z., Housa, D., Liska, F., Soltysová, L., Kaspárek, R., Bílá, V., Pravenec, M., Kren, V. Folia Biol. (Praha) (1999) [Pubmed]
  11. Differential distribution of vesicle associated membrane protein isoforms in the mouse retina. Sherry, D.M., Wang, M.M., Frishman, L.J. Mol. Vis. (2003) [Pubmed]
  12. Syndet, an adipocyte target SNARE involved in the insulin-induced translocation of GLUT4 to the cell surface. Rea, S., Martin, L.B., McIntosh, S., Macaulay, S.L., Ramsdale, T., Baldini, G., James, D.E. J. Biol. Chem. (1998) [Pubmed]
  13. Cleavage of SNAP-25 and VAMP-2 impairs store-operated Ca2+ entry in mouse pancreatic acinar cells. Rosado, J.A., Redondo, P.C., Salido, G.M., Sage, S.O., Pariente, J.A. Am. J. Physiol., Cell Physiol. (2005) [Pubmed]
  14. Molecular regulation of membrane resealing in 3T3 fibroblasts. Shen, S.S., Tucker, W.C., Chapman, E.R., Steinhardt, R.A. J. Biol. Chem. (2005) [Pubmed]
  15. Fusion-related release of glutamate from astrocytes. Zhang, Q., Pangrsic, T., Kreft, M., Krzan, M., Li, N., Sul, J.Y., Halassa, M., Van Bockstaele, E., Zorec, R., Haydon, P.G. J. Biol. Chem. (2004) [Pubmed]
  16. Reversible suppression of glutamatergic neurotransmission of cerebellar granule cells in vivo by genetically manipulated expression of tetanus neurotoxin light chain. Yamamoto, M., Wada, N., Kitabatake, Y., Watanabe, D., Anzai, M., Yokoyama, M., Teranishi, Y., Nakanishi, S. J. Neurosci. (2003) [Pubmed]
  17. Qualitative and quantitative differences between taste buds of the rat and mouse. Ma, H., Yang, R., Thomas, S.M., Kinnamon, J.C. BMC neuroscience (2007) [Pubmed]
  18. Regulation of insulin-stimulated GLUT4 translocation by Munc18c in 3T3L1 adipocytes. Thurmond, D.C., Ceresa, B.P., Okada, S., Elmendorf, J.S., Coker, K., Pessin, J.E. J. Biol. Chem. (1998) [Pubmed]
  19. The vesicle- and target-SNARE proteins that mediate Glut4 vesicle fusion are localized in detergent-insoluble lipid rafts present on distinct intracellular membranes. Chamberlain, L.H., Gould, G.W. J. Biol. Chem. (2002) [Pubmed]
  20. Functional studies in 3T3L1 cells support a role for SNARE proteins in insulin stimulation of GLUT4 translocation. Macaulay, S.L., Hewish, D.R., Gough, K.H., Stoichevska, V., MacPherson, S.F., Jagadish, M., Ward, C.W. Biochem. J. (1997) [Pubmed]
  21. GLUT4 overexpression or deficiency in adipocytes of transgenic mice alters the composition of GLUT4 vesicles and the subcellular localization of GLUT4 and insulin-responsive aminopeptidase. Carvalho, E., Schellhorn, S.E., Zabolotny, J.M., Martin, S., Tozzo, E., Peroni, O.D., Houseknecht, K.L., Mundt, A., James, D.E., Kahn, B.B. J. Biol. Chem. (2004) [Pubmed]
  22. Regional and progressive changes in brain expression of complexin II in a mouse transgenic for the Huntington's disease mutation. Freeman, W., Morton, A.J. Brain Res. Bull. (2004) [Pubmed]
  23. Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role in insulin-stimulated GLUT4 translocation. Widberg, C.H., Bryant, N.J., Girotti, M., Rea, S., James, D.E. J. Biol. Chem. (2003) [Pubmed]
  24. Adrenal gland SNAP-25 expression is altered in thyroid hormone receptor knock-out mice. Hepp, R., Grant, N.J., Espliguero, G., Aunis, D., Sarlieve, L.L., Rodrigues-Pena, A., Langley, K. Neuroreport (2001) [Pubmed]
  25. Fusion protein vesicle-associated membrane protein 2 is implicated in IFN-gamma-induced piecemeal degranulation in human eosinophils from atopic individuals. Lacy, P., Logan, M.R., Bablitz, B., Moqbel, R. J. Allergy Clin. Immunol. (2001) [Pubmed]
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