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
中科院分区:
文献类型:
--
作者:
Mim C;Cui H;Gawronski-Salerno JA;Frost A;Lyman E;Voth GA;Unger VM
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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影响因子:
64.5
作者:
Hurley JH;Boura E;Carlson LA;Różycki B
通讯作者:
Różycki B
影响因子:
11.8
作者:
Chang-Ileto, Belle;Frere, Samuel G.;Chan, Robin B.;Voronov, Sergey V.;Roux, Aurelian;Di Paolo, Gilbert
通讯作者:
Di Paolo, Gilbert
影响因子:
4.8
作者:
Jao, Christine C.;Hegde, Balachandra G.;Langen, Ralf
通讯作者:
Langen, Ralf
影响因子:
3
作者:
Sorzano, COS;Marabini, R;Pascual-Montano, A
通讯作者:
Pascual-Montano, A
DOI:
10.1042/bss0720223
发表时间:
2005-01-01
期刊:
LIPIDS, RAFTS AND TRAFFIC
影响因子:
--
作者:
Gallop, JL;McMahon, HT
通讯作者:
McMahon, HT