Control of neurotransmitter release by two distinct membrane-binding faces of the Munc13-1 C₁C₂B region.

ABSTRACT: Munc13-1 plays a central role in neurotransmitter release through its conserved C-terminal region, which includes a diacyglycerol (DAG)-binding C₁ domain, a Ca²⁺/PIP₂-binding C₂B domain, a MUN domain and a C₂C domain. Munc13-1 was proposed to bridge synaptic vesicles to the plasma membrane through distinct interactions of the C₁C₂B region with the plasma membrane: (i) one involving a polybasic face that is expected to yield a perpendicular orientation of Munc13-1 and hinder release; and (ii) another involving the DAG-Ca²⁺-PIP₂-binding face that is predicted to result in a slanted orientation and facilitate release. Here, we have tested this model and investigated the role of the C₁

SUBMITTER: Camacho M 

PROVIDER: S-EPMC8648301 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature