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Neuronal SNARE complex assembly guided by Munc18-1 and Munc13-1.

ABSTRACT: Neurotransmitter release by Ca²⁺ -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.

SUBMITTER: Wang S

PROVIDER: S-EPMC9623535 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature

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Neuronal SNARE complex assembly guided by Munc18-1 and Munc13-1.

Wang Shen S Ma Cong C

FEBS open bio 20220322 11

Neurotransmitter release by Ca<sup>2+</sup> -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 ...[more]

PMID: 35278279

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