期刊
STRUCTURE
卷 20, 期 5, 页码 874-886出版社
CELL PRESS
DOI: 10.1016/j.str.2012.03.008
关键词
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资金
- Department of Energy, Office of Biological and Environmental Research
- National Institutes of Health (NIH), National Center for Research Resources
- European Community
- Intramural AIDS Research Fellowship
- NIH, National Institute of Diabetes and Digestive and Kidney Diseases
- Office of the Director, NIH
- NIH [GM072694]
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 Forster 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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