Litcius/Paper detail

Neuronal SNARE complex assembly guided by Munc18‐1 and Munc13‐1

Shen Wang, Cong Ma

2022FEBS Open Bio24 citationsDOIOpen Access PDF

Abstract

-triggered synaptic vesicle exocytosis is essential for information transmission in the nervous system. The soluble N-ethylmaleimide sensitive factor attachment protein receptors (SNAREs) syntaxin-1, SNAP-25, and synaptobrevin-2 form the SNARE complex to bring synaptic vesicles and the plasma membranes together and to catalyze membrane fusion. Munc18-1 and Munc13-1 regulate synaptic vesicle priming via orchestrating neuronal SNARE complex assembly. In this review, we summarize recent advances toward the functions and molecular mechanisms of Munc18-1 and Munc13-1 in guiding neuronal SNARE complex assembly, and discuss the functional similarities and differences between Munc18-1 and Munc13-1 in neurons and their homologs in other intracellular membrane trafficking systems.

Topics & Concepts

SynaptobrevinExocytosisSNARE complexSynaptic vesicleMunc-18NeurotransmissionVesicle fusionLipid bilayer fusionCell biologyNeurotransmitterBiologyVesicleVesicular Transport ProteinsNeuroscienceChemistryIntracellularReceptorEndosomeMembraneBiochemistryCentral nervous systemVacuolar protein sortingCellular transport and secretionLipid Membrane Structure and BehaviorRetinal Development and Disorders