Neurotransmitters are released from synaptic and secretory vesicles following calcium-triggered fusion with the plasma membrane. These exocytotic events are driven by assembly of a ternary SNARE complex between the vesicle SNARE synaptobrevin and the plasma membrane-associated SNAREs syntaxin and SNAP-25. Proteins that affect SNARE complex assembly are therefore important regulators of synaptic strength. In this chapter, we review our current understanding of the roles played by two SNARE interacting proteins: UNC-13/Munc13 and UNC-18/Munc18. We discuss results from both invertebrate and vertebrate model systems, highlighting recent advances, focusing on the current consensus on molecular mechanisms of action and nanoscale organization, and pointing out some unresolved aspects of their functions.
Keywords: Docking; Exocytosis; Munc13; Munc18; Priming; SNAP-25; SNARE complex; Synaptic transmission; Synaptobrevin; Syntaxin.
© 2023. The Author(s), under exclusive license to Springer Nature Switzerland AG.