PMID: 9177194Jun 10, 1997Paper

Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesicles

Proceedings of the National Academy of Sciences of the United States of America
H OttoReinhard Jahn

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.

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Citations

Mar 25, 1999·Microscopy Research and Technique·D J EllisR M Henderson
Jun 16, 1999·Journal of Neuroscience Research·G GrosseM Bergmann
Jun 10, 1998·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·R D Burgoyne, A Morgan
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