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Complexin and Ca2+ stimulate SNARE-mediated membrane fusion.

ABSTRACT: Ca(2+)-triggered, synchronized synaptic vesicle fusion underlies interneuronal communication. Complexin is a major binding partner of the SNARE complex, the core fusion machinery at the presynapse. The physiological data on complexin, however, have been at odds with each other, making delineation of its molecular function difficult. Here we report direct observation of two-faceted functions of complexin using the single-vesicle fluorescence fusion assay and EPR. We show that complexin I has two opposing effects on trans-SNARE assembly: inhibition of SNARE complex formation and stabilization of assembled SNARE complexes. Of note, SNARE-mediated fusion is markedly stimulated by complexin, and it is further accelerated by two orders of magnitude in response to an externally applied Ca(2+) wave. We suggest that SNARE complexes, complexins and phospholipids collectively form a complex substrate for Ca(2+) and Ca(2+)-sensing fusion effectors in neurotransmitter release.

SUBMITTER: Yoon TY

PROVIDER: S-EPMC2493294 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature

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Complexin and Ca2+ stimulate SNARE-mediated membrane fusion.

Yoon Tae-Young TY Lu Xiaobing X Diao Jiajie J Lee Soo-Min SM Ha Taekjip T Shin Yeon-Kyun YK

Nature structural & molecular biology 20080615 7

Ca(2+)-triggered, synchronized synaptic vesicle fusion underlies interneuronal communication. Complexin is a major binding partner of the SNARE complex, the core fusion machinery at the presynapse. The physiological data on complexin, however, have been at odds with each other, making delineation of its molecular function difficult. Here we report direct observation of two-faceted functions of complexin using the single-vesicle fluorescence fusion assay and EPR. We show that complexin I has two ...[more]

PMID: 18552825

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