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• W2090217534 abstract "Trans-QabcR-SNARE pairing on opposing membranes is crucial for eukaryotic membrane fusion, but how selective pairs of Qabc- and R-SNARE proteins regulate membrane fusion specificity remains elusive. Here, we studied 14 purified full-length SNAREs that function in yeast endoplasmic reticulum (ER)-Golgi, intra-Golgi, endosomal and vacuolar transport by comprehensively testing cis-QabcR-SNARE assembly and fusogenicity of reconstituted SNARE proteoliposomes. Strikingly, the cognate ER-Golgi and intra-Golgi SNARE-complex assemblies were highly stringent, whereas endosomal and vacuolar SNAREs assembled rather promiscuously into the non-cognate mixed complexes. However, these patterns of cis-SNARE assemblies cannot solely explain their potency to be fusogenic via trans-SNARE pairing: Only the vacuolar 3Q-SNARE combination is fusogenic in the absence of additional components; endosomal SNARE-dependent fusogenicity requires membrane-tethering factors; and ER-Golgi SNAREs can be fusogenic by synergistic actions of tethering factors and the cognate Sec1/Munc18-family protein Sly1p. Thus, our findings uncover multiple and distinct strategies of SNAREs to directly mediate fusion specificity." @default.
• W2090217534 created "2016-06-24" @default.
• W2090217534 creator A5030785036 @default.
• W2090217534 creator A5073990082 @default.
• W2090217534 date "2014-03-04" @default.
• W2090217534 modified "2023-10-01" @default.
• W2090217534 title "Multiple and distinct strategies of yeast SNAREs to confer the specificity of membrane fusion" @default.
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• W2090217534 doi "https://doi.org/10.1038/srep04277" @default.
• W2090217534 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3940976" @default.
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• W2090217534 hasPublicationYear "2014" @default.
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