Structural basis of membrane bending by the N-BAR protein endophilin.

Structural basis of membrane bending by the N-BAR protein endophilin.
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DOI:
10.1016/j.cell.2012.01.048
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发表时间:
2012-03-30
期刊:
影响因子:
64.5
通讯作者:
Unger VM
Unger VM
中科院分区:
生物学1区
文献类型:
--
作者:
Mim C;Cui H;Gawronski-Salerno JA;Frost A;Lyman E;Voth GA;Unger VM

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Functioning as key players in cellular regulation of membrane curvature, BAR-domain proteins bend bilayers and recruit interaction partners through poorly understood mechanisms. Using electron cryomicroscopy, we present reconstructions of full-length endophilin and its N-terminal N-BAR domain in their membrane-bound state. Endophilin lattices expose large areas of membrane surface, and are held together by promiscuous interactions between endophilin's amphipathic N-terminal helices. Coarse-grained molecular dynamics simulations reveal that endophilin lattices are highly dynamic, and that the N-terminal helices are required for formation of a stable and regular scaffold. Furthermore, endophilin accommodates different curvatures through a quantized addition or removal of endophilin dimers, which in some cases causes dimerization of endophilin's SH3 domains, suggesting that the spatial presentation of SH3-domains rather than affinity governs the recruitment of downstream interaction partners.
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