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Review
. 2014 Jan 14:2:388-94.
doi: 10.1016/j.redox.2013.12.029. eCollection 2014.

The proteasome and the degradation of oxidized proteins: part III-Redox regulation of the proteasomal system

Tobias Jung Annika Höhn  1 , Tilman Grune  1
Affiliations
Review

The proteasome and the degradation of oxidized proteins: part III-Redox regulation of the proteasomal system

Tobias Jung Annika Höhn et al. Redox Biol. .

Abstract

Here, we review shortly the current knowledge on the regulation of the proteasomal system during and after oxidative stress. After addressing the components of the proteasomal system and the degradation of oxidatively damaged proteins in part I and II of this series, we address here which changes in activity undergo the proteasome and the ubiquitin-proteasomal system itself under oxidative conditions. While several components of the proteasomal system undergo direct oxidative modification, a number of redox-regulated events are modulating the proteasomal activity in a way it can address the major tasks in an oxidative stress situation: the removal of oxidized proteins and the adaptation of the cellular metabolism to the stress situation.

Keywords: 20S proteasome; Jak/Stat; Nrf2; PARP1; Ubiquitin–proteasome-system.

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Figures

Fig. 1
Fig. 1
Oxidative modifications of the proteasomal system.
Fig. 2
Fig. 2
De novo synthesis of the proteasomal system via Nrf2-mediated stress-response.
Fig. 3
Fig. 3
Jak/STAT-mediated induction of the inducible proteasome and PA28α/β.
Fig. 4
Fig. 4
Nuclear PARP-1-mediated proteasomal activation.
Fig. 5
Fig. 5
Response of the proteasomal system to oxidative stress.
See this image and copyright information in PMC

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