Matches in SemOpenAlex for { <https://semopenalex.org/work/W2951496883> ?p ?o ?g. }
- W2951496883 abstract "Sec1/Munc18-family (SM) proteins are required for SNARE-mediated membrane fusion, but their mechanism(s) of action remain controversial. Using single-molecule force spectroscopy, we found that the SM protein Munc18-1 catalyzes step-wise zippering of three synaptic SNAREs (syntaxin, VAMP2, and SNAP-25) into a four-helix bundle. Catalysis requires formation of an intermediate template complex in which Munc18-1 juxtaposes the N-terminal regions of the SNARE motifs of syntaxin and VAMP2, while keeping their C-terminal regions separated. SNAP-25 binds the templated SNAREs to induce full SNARE zippering. Munc18-1 mutations modulate the stability of the template complex in a manner consistent with their effects on membrane fusion, indicating that chaperoned SNARE assembly is essential for exocytosis. Two other SM proteins, Munc18-3 and Vps33, similarly chaperone SNARE assembly via a template complex, suggesting that SM protein mechanism is conserved." @default.
- W2951496883 created "2019-06-27" @default.
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- W2951496883 date "2018-12-12" @default.
- W2951496883 modified "2023-10-02" @default.
- W2951496883 title "Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association" @default.
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- W2951496883 doi "https://doi.org/10.7554/elife.41771" @default.
- W2951496883 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6320071" @default.
- W2951496883 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30540253" @default.
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