Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs - PubMed (original) (raw)
. 2004 Apr 16;304(5669):435-8.
doi: 10.1126/science.1097196. Epub 2004 Mar 25.
Affiliations
- PMID: 15044754
- DOI: 10.1126/science.1097196
Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs
Ward C Tucker et al. Science. 2004.
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.
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