Special Issue
Oxidative Stress-Mediated Regulation of Proteasome Complexes*

https://doi.org/10.1074/mcp.M110.006924Get rights and content
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Oxidative stress has been implicated in aging and many human diseases, notably neurodegenerative disorders and various cancers. The reactive oxygen species that are generated by aerobic metabolism and environmental stressors can chemically modify proteins and alter their biological functions. Cells possess protein repair pathways to rescue oxidized proteins and restore their functions. If these repair processes fail, oxidized proteins may become cytotoxic. Cell homeostasis and viability are therefore dependent on the removal of oxidatively damaged proteins. Numerous studies have demonstrated that the proteasome plays a pivotal role in the selective recognition and degradation of oxidized proteins. Despite extensive research, oxidative stress-triggered regulation of proteasome complexes remains poorly defined. Better understanding of molecular mechanisms underlying proteasome function in response to oxidative stress will provide a basis for developing new strategies aimed at improving cell viability and recovery as well as attenuating oxidation-induced cytotoxicity associated with aging and disease. Here we highlight recent advances in the understanding of proteasome structure and function during oxidative stress and describe how cells cope with oxidative stress through proteasome-dependent degradation pathways.

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*

This work was supported by National Institutes of Health grants (Epilepsy Research Training Program at UCI_T32 NS045540-06A1 to C. A. and GM-74830 to L. H.).

1

The abbreviations used are:

    ROS

    reactive oxygen species

    CP

    core particle

    PIP

    proteasome interacting protein

    GSH

    glutathione.