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Science. 2004 Apr 16;304(5669):435-8. Epub 2004 Mar 25.

Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs.

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  • 1Department of Physiology, University of Wisconsin, Madison, WI 53706, USA.

Abstract

We investigated the effect of synaptotagmin I on membrane fusion mediated by neuronal SNARE proteins, SNAP-25, syntaxin, and synaptobrevin, which were reconstituted into vesicles. In the presence of Ca2+, the cytoplasmic domain of synaptotagmin I (syt) strongly stimulated membrane fusion when synaptobrevin densities were similar to those found in native synaptic vesicles. The Ca2+ dependence of syt-stimulated fusion was modulated by changes in lipid composition of the vesicles and by a truncation that mimics cleavage of SNAP-25 by botulinum neurotoxin A. Stimulation of fusion was abolished by disrupting the Ca2+-binding activity, or by severing the tandem C2 domains, of syt. Thus, syt and SNAREs are likely to represent the minimal protein complement for Ca2+-triggered exocytosis.

PMID:
15044754
[PubMed - indexed for MEDLINE]
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