Molecular Mechanisms Underlying Neurotransmitter Release.
Annu Rev Biophys
; 51: 377-408, 2022 05 09.
Article
in En
| MEDLINE
| ID: mdl-35167762
ABSTRACT
Major recent advances and previous data have led to a plausible model of how key proteins mediate neurotransmitter release. In this model, the soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor (SNARE) proteins syntaxin-1, SNAP-25, and synaptobrevin form tight complexes that bring the membranes together and are crucial for membrane fusion. NSF and SNAPs disassemble SNARE complexes and ensure that fusion occurs through an exquisitely regulated pathway that starts with Munc18-1 bound to a closed conformation of syntaxin-1. Munc18-1 also binds to synaptobrevin, forming a template to assemble the SNARE complex when Munc13-1 opens syntaxin-1 while bridging the vesicle and plasma membranes. Synaptotagmin-1 and complexin bind to partially assembled SNARE complexes, likely stabilizing them and preventing fusion until Ca2+ binding to synaptotagmin-1 causes dissociation from the SNARE complex and induces interactions with phospholipids that help trigger release. Although fundamental questions remain about the mechanism of membrane fusion, these advances provide a framework to investigate the mechanisms underlying presynaptic plasticity.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
SNARE Proteins
/
Nerve Tissue Proteins
Type of study:
Prognostic_studies
Language:
En
Journal:
Annu Rev Biophys
Journal subject:
BIOFISICA
Year:
2022
Document type:
Article