InterPro domain: IPR016444

This entry includes vesicle-associated membrane proteins VAMP1/synaptobrevin-1, VAMP2/synaptobrevin-2, VAMP3/synaptobrevin-3 and VAMP8/endobrevin.

VAMPs are a group of small, integral membrane proteins of synaptic vesicles that is mostly involved in vesicle fusion. The heterotrimeric SNARE complex isformed by syntaxin 1, synaptosomal-associated protein 25kDa (SNAP25), and vesicle-associated membrane protein (VAMP)/synaptobrevin [ 1 ]. VAMP1 plays an essential, non-redundant role in Ca2+-triggered vesicle exocytosis at the mouse neuromuscular junction [ 2 ]. VAMP2 is extensively expressed in the central nervous system [ 3 ]. Neurotransmitter release involves the assembly of a heterotrimeric SNARE complex composed of SNAP25, VAMP2 and syntaxin 1 [ 4 ]. VAMP8 may be involved in regulated exocytosis of the exocrine system [ 4 , 5 ].

1. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-18
2. The role of synaptobrevin1/VAMP1 in Ca2+-triggered neurotransmitter release at the mouse neuromuscular junction. J. Physiol. (Lond.) 589, 1603-18
3. Calmodulin and lipid binding to synaptobrevin regulates calcium-dependent exocytosis. EMBO J. 21, 3970-9
4. A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar cells. Dev. Cell 7, 359-71
5. VAMP8/endobrevin as a general vesicular SNARE for regulated exocytosis of the exocrine system. Mol. Biol. Cell 18, 1056-63