Analysis of tripartite Synaptotagmin-1-SNARE-complexin-1 complexes in solution.

ABSTRACT: Characterizing interactions of Synaptotagmin-1 with the SNARE complex is crucial to understand the mechanism of neurotransmitter release. X-ray crystallography revealed how the Synaptotagmin-1 C₂ B domain binds to the SNARE complex through a so-called primary interface and to a complexin-1-SNARE complex through a so-called tripartite interface. Mutagenesis and electrophysiology supported the functional relevance of both interfaces, and extensive additional data validated the primary interface. However, ITC evidence suggesting that binding via the tripartite interface occurs in solution was called into question by subsequent NMR data. Here, we describe joint efforts to address this apparent contradiction. Using the same ITC approach with the same C₂ B domain mutant use

SUBMITTER: Jaczynska K 

PROVIDER: S-EPMC9811660 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature