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首页> 外文期刊>EMBO Journal >Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms
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Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms

机译：Endophilin酒吧域驱动膜曲率两个新发现的基于结构的机制

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摘要

The crescent-shaped BAR ( Bin/Amphiphysin/Rvs-homology) domain dimer is a versatile protein module that senses and generates positive membrane curvature. The BAR domain dimer of human endophilin-A1, solved at 3.1 angstrom, has a unique structure consisting of a pair of helix-loop appendages sprouting out from the crescent. The appendage's short helices form a hydrophobic ridge, which runs across the concave surface at its center. Examining liposome binding and tubulation in vitro using purified BAR domain and its mutants indicated that the ridge penetrates into the membrane bilayer and enhances liposome tubulation. BAR domain-expressing cells exhibited marked plasma membrane tubulation in vivo. Furthermore, a swinging-arm mutant lost liposome tubulation activity yet retaining liposome binding. These data suggested that the rigid crescent dimer shape is crucial for the tubulation. We here propose that the BAR domain drives membrane curvature by coordinate action of the crescent's scaffold mechanism and the ridge's membrane insertion in addition to membrane binding via amino-terminal amphipathic helix.
机译：新月形的栏(Bin / Amphiphysin / Rvs-homology)域二聚体是一个感觉和多功能蛋白质模块产生积极的膜曲率。人类endophilin-A1域二聚体,解决了3.1埃,有独特的结构组成一对helix-loop附属物发芽新月。形成一个疏水脊,在运行在其中心凹表面。绑定和制管体外使用纯化酒吧域及其突变体表示岭渗透入双层膜提高脂质体制管。domain-expressing细胞表现出显著的等离子体膜制管体内。摆动臂突变失去了脂质体制管活动还保留脂质体绑定。数据表明,刚性新月二聚体制管的形状是至关重要的。建议栏域驱动膜新月的曲率的协调行动脚手架机制和山脊的膜通过插入除了膜绑定伴两亲的螺旋。

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