Synaptic Vesicles Position Complexin to Block Spontaneous Fusion

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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 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. 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.

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Wragg, R. T., Snead, D., Dong, Y., Ramlall, T. F., Menon, I., Bai, J., … Dittman, J. S. (2013). Synaptic Vesicles Position Complexin to Block Spontaneous Fusion. Neuron, 77(2), 323–334. https://doi.org/10.1016/j.neuron.2012.11.005

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