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Nat Rev Mol Cell Biol. 2014 Feb;15(2):122-33. doi: 10.1038/nrm3741.

Regulated protein turnover: snapshots of the proteasome in action.

Author information

1
Department of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, USA.
2
1] Department of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, USA. [2] Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin, Texas 78712, USA.

Abstract

The ubiquitin proteasome system (UPS) is the main ATP-dependent protein degradation pathway in the cytosol and nucleus of eukaryotic cells. At its centre is the 26S proteasome, which degrades regulatory proteins and misfolded or damaged proteins. In a major breakthrough, several groups have determined high-resolution structures of the entire 26S proteasome particle in different nucleotide conditions and with and without substrate using cryo-electron microscopy combined with other techniques. These structures provide some surprising insights into the functional mechanism of the proteasome and will give invaluable guidance for genetic and biochemical studies of this key regulatory system.

PMID:
24452470
PMCID:
PMC4384331
DOI:
10.1038/nrm3741
[Indexed for MEDLINE]
Free PMC Article
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