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Synaptic vesicles position complexin to block spontaneous fusion.


ABSTRACT: Synapses continually replenish their synaptic vesicle (SV) pools while suppressing spontaneous fusion events, thus maintaining a high dynamic range in response to physiological stimuli. The presynaptic protein complexin can both promote and inhibit fusion through interactions between its ?-helical domain and the SNARE complex. In addition, complexin's C-terminal half is required for the inhibition of spontaneous fusion in worm, fly, and mouse, although the molecular mechanism remains unexplained. We show here that complexin's C-terminal domain binds lipids through a novel protein motif, permitting complexin to inhibit spontaneous exocytosis in vivo by targeting complexin to SVs. We propose that the SV pool serves as a platform to sequester and position complexin where it can intercept the rapidly assembling SNAREs and control the rate of spontaneous fusion.

SUBMITTER: Wragg RT 

PROVIDER: S-EPMC3559010 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature

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Synaptic vesicles position complexin to block spontaneous fusion.

Wragg Rachel T RT   Snead David D   Dong Yongming Y   Ramlall Trudy F TF   Menon Indu I   Bai Jihong J   Eliezer David D   Dittman Jeremy S JS  

Neuron 20130101 2


Synapses continually replenish their synaptic vesicle (SV) pools while suppressing spontaneous fusion events, thus maintaining a high dynamic range in response to physiological stimuli. The presynaptic protein complexin can both promote and inhibit fusion through interactions between its α-helical domain and the SNARE complex. In addition, complexin's C-terminal half is required for the inhibition of spontaneous fusion in worm, fly, and mouse, although the molecular mechanism remains unexplained  ...[more]

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