Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion.
Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion.
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DOI：
10.1038/nsmb.1433
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发表时间：
2008-07
影响因子：
16.8
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中科院分区：
文献类型：
--
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可溶性 N-乙基马来酰亚胺敏感因子附着蛋白受体 (SNARE) 复合物的形成促进细胞内膜融合。单一的 SNARE 复合体被认为是不够的； SNARE 复合体的多个副本必须协同工作。然而，这种高阶 SNARE 蛋白质结构的组装机制尚不清楚。 EPR 和荧光分析表明，至少三个拷贝的靶膜 SNARE 蛋白通过跨膜结构域 (TMD) 之间的相互作用进行自组装，并且这种多聚体结构充当反 SNARE 组装的支架。溶液中 SNARE 核心的形成诱导相邻膜中囊泡相关 SNARE 的 TMD 寡聚化，瞬时形成跨越两个膜的超分子蛋白质结构。这种高阶蛋白质中间体通过涉及脂质分子而进化到半融合状态。半融合之后是远端小叶混合并形成顺式圈套复合体。
Formation of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex facilitates intracellular membrane fusion. A single SNARE complex is thought to be insufficient; multiple copies of SNARE complexes must work cooperatively. However, the mechanism by which such a higher-order SNARE protein structure is assembled is unknown. EPR and fluorescence analyses show that at least three copies of target-membrane SNARE proteins self-assemble through the interaction between the transmembrane domains (TMDs), and this multimeric structure serves as scaffolding for trans-SNARE assembly. SNARE core formation in solution induces oligomerization of the TMDs of vesicle-associated SNAREs in the apposing membrane, transiently forming a supramolecular protein structure spanning two membranes. This higher-order protein intermediate evolves, by involving lipid molecules, to the hemifusion state. Hemifusion is subsequently followed by distal leaflet mixing and formation of the cis-SNARE complex.
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