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Mutations of Single Residues in the Complexin N-terminus Exhibit Distinct Phenotypes in Synaptic Vesicle Fusion
Mutations of Single Residues in the Complexin N-terminus Exhibit Distinct Phenotypes in Synaptic Vesicle Fusion Estelle Toulme, Jacqueline Murach, Simon Bärfuss, Jana Kroll, Jörg Malsam, Thorsten Trimbuch, Melissa A. Herman, Thomas H. Söllner, Christian Rosenmund Journal of Neuroscience 31 July 2024, 44 (31) e0076242024; DOI: 10.1523/JNEUROSCI.0076-24.2024
Mutations of single residues in the complexin N-terminus exhibit distinct phenotypes in synaptic vesicle fusion
Abstract The release of neurotransmitters at central synapses is dependent on a cascade of protein interactions, specific to the presynaptic compartment. Amongst those dedicated molecules, the cytosolic complexins play an incompletely defined role as synaptic transmission regulators. Complexins are multidomain proteins that bind SNARE complexes, conferring both inhibitory and stimulatory functions.
Complexin Suppresses Spontaneous Exocytosis by Capturing the Membrane-Proximal Regions of VAMP2 and SNAP25
Highlights • Detection of a bipartite complexin accessory helix-SNARE interface prior to fusion • The Cpx-SNARE interface suppresses SNARE complex zippering • The interface contributes to clamp spontaneous neurotransmitter release Summary The neuronal protein complexin contains multiple domains that exert clamping and facilitatory functions to tune spontaneous and action potential-triggered synaptic release.
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