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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Munc18-1 binds directly to the neuronal SNARE complex
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Munc18-1 binds directly to the neuronal SNARE complex

机译：Munc18-1直接结合神经元SNARE复合体

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摘要

Both SM proteins (for Sec1/Munc18-like proteins) and SNARE proteins (for soluble NSF-attachment protein receptors) are essential for intracellular membrane fusion, but the general mechanism of coupling between their functions is unclear, in part because diverse SM protein/SNARE binding modes have been described. During synaptic vesicle exocytosis, the SM protein Munc18-1 is known to bind tightly to the SNARE protein syntaxin-1, but only when syntaxin-1 is in a closed conformation that is incompatible with SNARE complex formation. We now show that Munc18-1 also binds tightly to assembled SNARE complexes containing syntaxin-1. The newly discovered Munc18-1/SNARE complex interaction involves contacts of Munc18-1 with the N-terminal H_(abc) domain of syntaxin-1 and the four-helical bundle of the assembled SNARE complex. Together with earlier studies, our results suggest that binding of Munc18-1 to closed syntaxin-1 is a specialization that evolved to meet the strict regulatory requirements of neuronal exocytosis, whereas binding of Munc18-1 to assembled SNARE complexes reflects a general function of SM proteins involved in executing membrane fusion.
机译：SM蛋白（用于Sec1 / Munc18样蛋白）和SNARE蛋白（用于可溶性NSF附着蛋白受体）对于细胞内膜融合都是必不可少的，但其功能之间的偶联一般机制尚不清楚，部分原因是因为多种SM蛋白/ SNARE绑定模式已被描述。在突触小泡胞吐过程中，已知SM蛋白Munc18-1与SNARE蛋白syntaxin-1紧密结合，但是只有当syntaxin-1处于与SNARE复合物形成不相容的闭合构象时。现在，我们显示Munc18-1还与包含语法1的组装后的SNARE复合物紧密结合。新发现的Munc18-1 / SNARE复合体相互作用涉及Munc18-1与Syntaxin-1的N端H_（abc）域和组装的SNARE复合体的四螺旋束的接触。与早期的研究一起，我们的结果表明，Munc18-1与闭合的syntaxin-1的结合是一种专一性，可以满足神经元胞吐作用的严格调节要求，而Munc18-1与组装的SNARE复合物的结合反映了SM的一般功能。参与膜融合的蛋白质。

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