Solution structure of the ESCRT-I and -II supercomplex: implications for membrane budding and scission.

Solution structure of the ESCRT-I and -II supercomplex: implications for membrane budding and scission.
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DOI:
10.1016/j.str.2012.03.008
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发表时间:
2012-05-09
期刊:
影响因子:
5.7
通讯作者:
Hurley, James H.
Hurley, James H.
中科院分区:
生物学2区
文献类型:
--
作者:
Boura, Evzen;Rozycki, Bartosz;Chung, Hoi Sung;Herrick, Dawn Z.;Canagarajah, Bertram;Cafiso, David S.;Eaton, William A.;Hummer, Gerhard;Hurley, James H.

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ESCRT-I和ESCRT-II超复合物诱导内陷到内体内腔的膜芽,这是泛素化膜蛋白的溶酶体降解的中心过程。对小角X射线散射(SAXS),单分子Förster共振能量转移(smFRET),和双电子-电子共振(DEER)光谱的溶液构象的膜出芽ESCRT-I-II超复合物从酵母精制。这些改进产生了18个ESCRT-I-II超复杂结构的集合,其范围从紧凑到高度扩展。ESCRT-I-II超复合物结构的新月形形状为详细的机理模型提供了基础,其中ESCRT-I-II通过内衬新生芽颈的孔来稳定膜芽并协调货物分选。本文所用的混合精化方法是通用的,也适用于其它动态多蛋白质组装。
The ESCRT-I and ESCRT-II supercomplex induces membrane buds that invaginate into the lumen of endosomes, a process central to the lysosomal degradation of ubiquitinated membrane proteins. The solution conformation of the membrane-budding ESCRT-I-II supercomplex from yeast was refined against small-angle X-ray scattering (SAXS), single-molecule Förster resonance energy transfer (smFRET), and double electron-electron resonance (DEER) spectra. These refinements yielded an ensemble of 18 ESCRT-I-II supercomplex structures that range from compact to highly extended. The crescent shapes of the ESCRT-I-II supercomplex structures provide the basis for a detailed mechanistic model, in which ESCRT-I-II stabilizes membrane buds and coordinates cargo sorting by lining the pore of the nascent bud necks. The hybrid refinement used here is general and should be applicable to other dynamic multiprotein assmeblies.
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