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• W2910595951 abstract "Abstract The transition of the Munc18-1/syntaxin-1 complex to the SNARE complex, a key step involved in exocytosis, is regulated by Munc13-1, SNAP-25 and synaptobrevin-2, but the underlying mechanism remains elusive. Here, we identify an interaction between Munc13-1 and the membrane-proximal linker region of synaptobrevin-2, and reveal its essential role in transition and exocytosis. Upon this interaction, Munc13-1 not only recruits synaptobrevin-2-embedded vesicles to the target membrane but also renders the synaptobrevin-2 SNARE motif more accessible to the Munc18-1/syntaxin-1 complex. Afterward, the entry of SNAP-25 leads to a half-zippered SNARE assembly, which eventually dissociates the Munc18-1/syntaxin-1 complex to complete SNARE complex formation. Our data suggest that Munc18-1 and Munc13-1 together serve as a functional template to orchestrate SNARE complex assembly." @default.
• W2910595951 created "2019-01-25" @default.
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• W2910595951 date "2019-01-08" @default.
• W2910595951 modified "2023-09-29" @default.
• W2910595951 title "Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly" @default.
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• W2910595951 doi "https://doi.org/10.1038/s41467-018-08028-6" @default.
• W2910595951 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6325239" @default.
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