Reconstitution of Ca2+-Regulated Membrane Fusion by Synaptotagmin and SNAREs

Ward C. Tucker, Thomas Weber, Edwin R. Chapman

Research output: Contribution to journalArticlepeer-review

305 Scopus citations

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.

Original languageEnglish
Pages (from-to)435-438
Number of pages4
JournalScience
Volume304
Issue number5669
DOIs
StatePublished - 16 Apr 2004

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