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• W2002095327 startingPage "6197" @default.
• W2002095327 abstract "The synaptic membrane proteins synaptobrevin, syntaxin, and SNAP-25 form a ternary complex that can be disassembled by the ATPase N-ethylmaleimide-sensitive factor (NSF) in the presence of soluble cofactors (SNAP proteins). These steps are thought to represent molecular events involved in docking and subsequent exocytosis of synaptic vesicles. Using two independent and complementary approaches, we now report that such ternary complexes form in the membrane of highly purified and monodisperse synaptic vesicles in the absence of the plasma membrane. Furthermore, the complexes are reversibly dissociated by NSF and SNAP proteins. Thus, ternary complexes can be assembled and disassembled while all three proteins are anchored as neighbors in the same membrane, suggesting that NSF is involved in priming synaptic vesicles for exocytosis." @default.
• W2002095327 created "2016-06-24" @default.
• W2002095327 creator A5020475421 @default.
• W2002095327 creator A5067052028 @default.
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• W2002095327 date "1997-06-10" @default.
• W2002095327 modified "2023-10-02" @default.
• W2002095327 title "Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesicles" @default.
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• W2002095327 doi "https://doi.org/10.1073/pnas.94.12.6197" @default.
• W2002095327 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/21026" @default.
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