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Vesicle-associated membrane protein

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Synaptobrevin
Three different views of the high resolution structure of a truncated neuronal SNARE complex. Legend: synaptobrevin-2 (red), Syntaxin-1 (pink), SNAP-25 (purple).
Identifiers
SymbolSynaptobrevin
PfamPF00957
InterProIPR016444
PROSITEPDOC00368
SCOP21sfc / SCOPe / SUPFAM
OPM superfamily197
OPM protein4wy4
Membranome198
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Hypothetic models of VAMP2 conformations and engagement in SNARE complex assembly for neurotransmitter release

Vesicle associated membrane proteins (VAMPs) are a family of SNARE proteins with similar structure, and are mostly involved in vesicle fusion.

  • VAMP1 and VAMP2 proteins known as synaptobrevins are expressed in brain and are constituents of the synaptic vesicles, where they participate in neurotransmitter release.
  • VAMP3 (known as cellubrevin) is ubiquitously expressed and participates in regulated and constitutive exocytosis as a constituent of secretory granules and secretory vesicles.
  • VAMP5 and VAMP7 participate in constitutive exocytosis.
    • VAMP5 is a constituent of secretory vesicles, myotubes and tubulovesicular structures.
    • VAMP7 is found both in secretory granules and endosomes.
  • VAMP8 (known as endobrevin) participates in endocytosis and is found in early endosomes. VAMP8 also participates the regulated exocytosis in pancreatic acinar cells.
  • VAMP4 is involved in transport from the Golgi.[1]

References

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  1. ^ Steegmaier M, Klumperman J, Foletti DL, Yoo JS, Scheller RH (1999). "Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle trafficking". Mol. Biol. Cell. 10 (6): 1957–72. doi:10.1091/mbc.10.6.1957. PMC 25394. PMID 10359608.
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