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Publication : Interaction of the Complexin Accessory Helix with Synaptobrevin Regulates Spontaneous Fusion.

First Author  Vasin Alexander Year  2016
Journal  Biophys. J. Volume  111
Pages  1954-1964 PubMed ID  27806277
Abstract Text  3-69paralytic mutant, which has a single-point mutation in the t-SNARE and displays enhanced spontaneous release. MD simulations demonstrated an altered interaction of Cpx with the SNARE bundle that hindered v-SNARE unraveling by Cpx, thus compromising clamping. We used our model to predict mutations that should enhance the ability of Cpx to prevent full assembly of the SNARE complex. MD simulations predicted that a weakened interaction between the Cpx accessory helix and the v-SNARE would enhance Cpx flexibility and thus promote separation of SNAREs, reducing spontaneous fusion. We generated transgenic Drosophila with mutations in Cpx and the v-SNARE that disrupted a salt bridge between these two proteins. As predicted, both lines demonstrated a selective inhibition in spontaneous release, suggesting that Cpx acts as a fusion clamp that restricts full SNARE zippering. Doi  10.1016/j.bpj.2016.09.017
Issue  9 Month  Nov

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