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.
复制标题
DOI:
10.1016/j.str.2012.03.008
复制
发表时间:
2012-05-09
期刊:
影响因子:
5.7
通讯作者:
Hurley, James H.
中科院分区:
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.
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.
登录
查看更多内容
DOI:
10.1126/science.1161070
发表时间:
2008-09-05
期刊:
Science (New York, N.Y.)
影响因子:
--
作者:
Lata S;Schoehn G;Jain A;Pires R;Piehler J;Gottlinger HG;Weissenhorn W
通讯作者:
Weissenhorn W
DOI:
10.1038/nrm2937
发表时间:
2010-08
期刊:
Nature reviews. Molecular cell biology
影响因子:
--
作者:
通讯作者:
--
影响因子:
64.5
作者:
Katzmann, DJ;Babst, M;Emr, SD
通讯作者:
Emr, SD
影响因子:
56.9
作者:
Carlton, Jez G.;Martin-Serrano, Juan
通讯作者:
Martin-Serrano, Juan
影响因子:
11.4
作者:
Alam, SL;Sun, J;Sundquist, WI
通讯作者:
Sundquist, WI