Open AccessComplexin-1 Enhances the On-Rate of Vesicle Docking via Simultaneous SNARE and Membrane Interactions
Author(s) -
Jiajie Diao,
Daniel J. Cipriano,
Minglei Zhao,
Yunxiang Zhang,
Sachi Shah,
Mark Padolina,
Richard A. Pfuetzner,
Axel T. Brünger
Publication year - 2013
Publication title -
journal of the american chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.115
H-Index - 612
eISSN - 1520-5126
pISSN - 0002-7863
DOI - 10.1021/ja407392n
Subject(s) - synaptotagmin 1 , synaptic vesicle , chemistry , vesicle , snap25 , snare complex , syntaxin , vesicle fusion , microbiology and biotechnology , synaptobrevin , kiss and run fusion , biophysics , membrane , biochemistry , biology
In synaptic terminals, complexin is thought to have inhibitory and activating roles for spontaneous "mini" release and evoked synchronized neurotransmitter release, respectively. We used single vesicle-vesicle microscopy imaging to study the effect of complexin-1 on the on-rate of docking between vesicles that mimic synaptic vesicles and the plasma membrane. We found that complexin-1 enhances the on-rate of docking of synaptic vesicle mimics containing full-length synaptobrevin-2 and full-length synaptotagmin-1 to plasma membrane-mimicking vesicles containing full-length syntaxin-1A and SNAP-25A. This effect requires the C-terminal domain of complexin-1, which binds to the membrane, the presence of PS in the membrane, and the core region of complexin-1, which binds to the SNARE complex.
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