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


ABSTRACT: 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.

SUBMITTER: Boura E 

PROVIDER: S-EPMC3572543 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature

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

Boura Evzen E   Różycki Bartosz B   Chung Hoi Sung HS   Herrick Dawn Z DZ   Canagarajah Bertram B   Cafiso David S DS   Eaton William A WA   Hummer Gerhard G   Hurley James H JH  

Structure (London, England : 1993) 20120501 5


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  ...[more]

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