Molecular basis for Gβγ-SNARE-mediated inhibition of synaptic vesicle fusion.

ABSTRACT: Neurotransmitter release is a complex process involving tightly controlled co-factors and protein-protein interactions. G-protein coupled receptors negatively regulate exocytosis via the interaction of G-protein βγ (Gβγ) heterodimers with the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex. The neuronal ternary SNARE complex comprises synaptosomal-associated protein-25 (SNAP25), syntaxin-1A, and synaptobrevin-2. The regions of the SNARE complex that are important for interactions with Gβγ have been extensively characterized, but the critical sites on Gβγ are not well understood. Furthermore, the molecular basis for the specificity of different Gβ and Gγ isoforms for SNARE proteins remains elusive. Thus, we holistically probed the entire family of human

SUBMITTER: Eitel AR 

PROVIDER: S-EPMC12302718 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature