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Sci. Signal., 7 December 2010
Vol. 3, Issue 151, p. ra88
[DOI: 10.1126/scisignal.2001232]

RESEARCH ARTICLES

Editor's Summary

Separation of Powers
The proteasome is a large, multicatalytic complex that degrades proteins in an ATP- and ubiquitin-dependent manner. The 26S proteasome is composed of the 20S catalytic core and the 19S regulatory particle. The 19S particle consists of two subcomplexes that constitute the base and lid structures around the catalytic core. When separated from the 26S proteasome, the 20S core degrades oxidized (nonubiquitinated) proteins. Oxidative stress results in the accumulation of damaged proteins in the cell, which are removed by proteasomes. Wang et al. used mass spectrometry to examine the effects of hydrogen peroxide (H2O2)–induced stress on the 26S proteasome in yeast. H2O2 triggered recruitment to the 19S particle of the proteasome-binding protein Ecm29 and disassembly of the 26S proteasome into its 20S and 19S constituents. Yeast strains deficient in Ecm29 did not exhibit 26S disassembly and were more sensitive to H2O2 than were wild-type cells. Indeed, an efficient response to H2O2 required disassembly of the 26S proteasome to generate sufficient amounts of free 20S core to degrade oxidized proteins. Similar results were obtained in experiments with a human cell line, which suggests that dissociation of the 26S proteasome in response to oxidative stress may be a conserved cellular response in eukaryotes.

Citation: X. Wang, J. Yen, P. Kaiser, L. Huang, Regulation of the 26S Proteasome Complex During Oxidative Stress. Sci. Signal. 3, ra88 (2010).

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