Solution Structure of the ESCRT-I and -II Supercomplex: Implications for Membrane Budding and Scission

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• 作者：Evzen Boura¹ ; ⁴ ; Bartosz Ró ; ż ; ycki² ; ⁴ ; Hoi  ; Sung Chung² ; Dawn  ; Z. Herrick³ ; Bertram Canagarajah¹ ; David  ; S. Cafiso³ ; William  ; A. Eaton² ; Gerhard Hummer² ; ^{gerhard.hummer@nih.gov} ; James  ; H. Hurley¹ ; ^{hurley@helix.nih.gov}
• 刊名：Structure
• 出版年：2012
• 期刊代码：143_09692126
• 类别：bio
• 出版时间：9 May, 2012
• 卷：20
• 期：5
• 页码：874-886
• 文件大小：1547 K

摘要

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Summary

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聽ESCRT-I-II supercomplex from yeast was refined against small-angle X-ray scattering (SAXS), single-molecule F枚rster 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.