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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p
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Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p

机译：Sec1 / Munc-18蛋白Sec1p的特定SNARE复合体结合模式

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摘要

The Sec1/Munc-18 (SM) family of proteins is required for vesicle fusion in eukaryotic cells and has been linked to the membrane-fusion proteins known as soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). SM proteins may activate the target-membrane SNARE, syntaxin, for assembly into the fusogenic SNARE complex. In support of an activation role, SM proteins bind directly to their cognate syntaxins. An exception is the yeast Sec1p, which does not bind the yeast plasma-membrane syntaxin, Sso1p. This exception could be explained if the SM interaction motif were blocked by the highly stable closed conformation of Sso1p. We tested the possibility of a latent binding motif using sso1 mutants in yeast and reconstituted the Sec1p binding specificity observed in vivo with purified proteins in vitro. Our results indicate there is no latent binding motif in Sso1p. Instead, Sec1p binds specifically to the ternary SNARE complex, with no detectable binding to the binary t-SNARE complex or any of the three individual SNAREs in their uncomplexed forms. We propose that vesicle fusion requires a specific interaction between the SM protein and the ternary SNARE complex.
机译：Sec1 / Munc-18（SM）家族是真核细胞中囊泡融合所必需的蛋白质，已与称为可溶性N-乙基马来酰亚胺敏感因子附着蛋白受体（SNARE）的膜融合蛋白相连。 SM蛋白可以激活靶膜SNARE，syntaxin，从而组装成融合的SNARE复合体。为了支持激活作用，SM蛋白直接与其同源语法素结合。酵母Sec1p是一个例外，它不结合酵母血浆膜语法素Sso1p。如果SM相互作用基序被Sso1p的高度稳定的封闭构象所阻断，则可以解释这种例外情况。我们测试了在酵母中使用sso1突变体潜在结合基序的可能性，并用体外纯化的蛋白重建了体内观察到的Sec1p结合特异性。我们的结果表明Sso1p中没有潜在的结合基序。而是，Sec1p专门绑定到三元SNARE复合体，而未检测到二进制t-SNARE复合体或未复杂形式的三个单独的SNARE中的​​任何一个。我们建议囊泡融合需要SM蛋白和三元SNARE复杂之间的特定相互作用。

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