Heterodimerization of Munc13 C₂A domain with RIM regulates synaptic vesicle docking and priming.

ABSTRACT: The presynaptic active zone protein Munc13 is essential for neurotransmitter release, playing key roles in vesicle docking and priming. Mechanistically, it is thought that the C₂A domain of Munc13 inhibits the priming function by homodimerization, and that RIM disrupts the autoinhibitory homodimerization forming monomeric priming-competent Munc13. However, it is unclear whether the C₂A domain mediates other Munc13 functions in addition to this inactivation-activation switch. Here, we utilize mutations that modulate the homodimerization and heterodimerization states to define additional roles of the Munc13 C₂A domain. Using electron microscopy and electrophysiology in hippocampal cultures, we show that the C₂A domain is critical for additional ste

SUBMITTER: Camacho M 

PROVIDER: S-EPMC5436228 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature