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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphatases / metabolism
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Animals
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Carrier Proteins / metabolism
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Exocytosis
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Intracellular Membranes / metabolism
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Kinetics
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Membrane Proteins / chemistry
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Membrane Proteins / isolation & purification
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Membrane Proteins / metabolism*
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N-Ethylmaleimide-Sensitive Proteins
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / isolation & purification
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Nerve Tissue Proteins / metabolism*
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Qa-SNARE Proteins
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R-SNARE Proteins
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Synaptic Vesicles / metabolism*
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Synaptosomal-Associated Protein 25
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Synaptosomes / metabolism
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Vesicular Transport Proteins*
Substances
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Carrier Proteins
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Membrane Proteins
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Nerve Tissue Proteins
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Qa-SNARE Proteins
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R-SNARE Proteins
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Recombinant Proteins
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Synaptosomal-Associated Protein 25
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Vesicular Transport Proteins
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Adenosine Triphosphatases
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N-Ethylmaleimide-Sensitive Proteins