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Article

Genetic analysis of the Complexin trans-clamping model for cross-linking SNARE complexes in vivo.

Proceedings of the National Academy of Sciences of the United States of America - 15 Jul 2014

Cho Richard W, Kümmel Daniel, Li Feng, Baguley Stephanie Wood, Coleman Jeff, Rothman James E, Littleton J Troy

Abstract excerpt

Complexin (Cpx) is a SNARE-binding protein that regulates neurotransmission by clamping spontaneous synaptic vesicle fusion in the absence of Ca(2+) influx while promoting evoked release in response to an action potential. Previous studies indicated Cpx may cross-link multiple SNARE complexes via a trans interaction to function as a fusion clamp. During Ca(2+) influx, Cpx is predicted to undergo a conformational...

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Identifiers

PMID: 24982161
DOI: 10.1073/pnas.1409311111
PMCID: PMC4104896

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Genetic analysis of the Complexin trans-clamping model for cross-linking SNARE complexes in vivo.PMID 24982161Read ↗

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Mutations of Single Residues in the Complexin N-terminus Exhibit Distinct Phenotypes in Synaptic Vesicle Fusion.Semantic proximity Read ↗

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synaptotagmin mutants reveal essential functions for the C2B domain in Ca2+-triggered fusion and recycling of synaptic vesicles in vivo.Semantic proximity Read ↗

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Complexin Binding to Membranes and Acceptor t-SNAREs Explains Its Clamping Effect on Fusion.Semantic proximity Read ↗

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