- Synaptobrevin
Synaptobrevins ("synaptobrevin isotypes 1-2") are small
integral membrane proteins of secretory vesicles withmolecular weight of 18kilodalton (kDa) that are part of thevesicle-associated membrane protein (VAMP) family.cite journal
author = Baumert M, Maycox PR, Navone F, De Camilli P, Jahn R
url = http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=2498078
title = Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain
journal = EMBO J
volume = 8
issue =
pages = 379–384
year = 1989
pmid = 2498078] cite journal
author = Bock JB, Scheller RH
url = http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=10535902
title = SNARE proteins mediate lipid bilayer fusion
journal = PNAS
volume = 96
issue =
pages = 12227–12229
year = 1999
doi = 10.1073/pnas.96.22.12227
pmid = 10535902] cite journal
author = Ernst JA, Brunger AT
url = http://www.jbc.org/cgi/content/full/278/10/8630
title = High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex
journal = J Biol Chem
volume = 278
issue =
pages = 8630–8636
year = 2003
doi = 10.1074/jbc.M211889200
pmid = 12496247] cite journal
author = Fasshauer D, Sutton RB, Brunger AT, Jahn R
url = http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=9861047
title = Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
journal = PNAS
volume = 95
issue =
pages = 15781–15786
year = 1998
doi = 10.1073/pnas.95.26.15781
pmid = 9861047] cite journal
author = Weber T, Zemelman BV, McNew JA, Westermann B, Gmachl M, Parlati F, Sollner TH, Rothman JE
doi = 10.1016/S0092-8674(00)81404-X
title = SNAREpins: minimal machinery for membrane fusion
journal = Cell
volume = 92
issue =
pages = 759–772
year = 1998]Synaptobrevin is one of the
SNARE proteins involved in formation of the SNARE complexes.tructure
Out of four α-helices of the core SNARE complex one is contributed by synaptobrevin, one by
syntaxin , and two bySNAP-25 (in neurons).Function
SNARE proteins are the key components of the molecular machinery that drives fusion of membranes in
exocytosis . Their function however is subject to fine tuning by various regulatory protein collectively referred to as "SNARE masters".Classification
Because all proteins belonging to VAMP/synaptobrevin family share common structural feature, they have been classified as
R-SNAREs . An alternative classification (v- and t-SNAREs) exists that takes into account origin of synaptobrevin-bearing organelle rather than their structural properties.Clinical significance
Synaptobrevin is degraded by "
Tetanospasmin ", a protein derived from "Clostridium tetani ".References and notes
External links
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