Complexin Suppresses Spontaneous Exocytosis by Capturing the Membrane-Proximal 
Regions of VAMP2 and SNAP25

Malsam, J.; Barfuss, S.; Trimbuch, T.; Zarebidaki, F.; Sonnen, A. F. P.; Wild, K.; Scheutzow, A.; Rohland, L.; Mayer, M. P.; Sinning, I.; Briggs, John A. G.; Rosenmund, C.; Sollner, T. H.

doi:10.1016/j.celrep.2020.107926

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Complexin Suppresses Spontaneous Exocytosis by Capturing the Membrane-Proximal Regions of VAMP2 and SNAP25

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Malsam, J., Barfuss, S., Trimbuch, T., Zarebidaki, F., Sonnen, A. F. P., Wild, K., et al. (2020). Complexin Suppresses Spontaneous Exocytosis by Capturing the Membrane-Proximal Regions of VAMP2 and SNAP25. Cell Reports, 32(3): 107926. doi:10.1016/j.celrep.2020.107926.

Cite as: https://hdl.handle.net/21.11116/0000-0009-7235-B

Abstract

The neuronal protein complexin contains multiple domains that exert clamping and facilitatory functions to tune spontaneous and action potential-triggered synaptic release. We address the clamping mechanism and show that the accessory helix of complexin arrests assembly of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex that forms the core machinery of intracellular membrane fusion. In a reconstituted fusion assay, site- and stage-specific photo-cross-linking reveals that, prior to fusion, the complexin accessory helix laterally binds the membrane-proximal C-terminal ends of SNAP25 and VAMP2, Corresponding complexin interface mutants selectively increase spontaneous release of neurotransmitters in living neurons, implying that the accessory helix suppresses final zippering/assembly of the SNARE four-helix bundle by restraining VAMP2 and SNAP25.