New EMBO Members Review
- The EMBO Journal (2005) 24, 1311 - 1317
- doi:10.1038/sj.emboj.7600599
Published online: 3 March 2005
Subject Category:
Role of oxidative carbonylation in protein quality control and senescence
Thomas Nyström1
- Department of Cell and Molecular Biology–Microbiology, Göteborg University, Göteborg, Sweden
Correspondence to:
Thomas Nyström, Department of Cell and Molecular Biology, Göteborg University, Medicinaregatan 9C, 413 90 Göteborg, Sweden. Tel.: +46 31 7732582; Fax: +46 31 7732599; E-mail: thomas.nystrom@gmm.gu.se
Received 8 December 2004; Accepted 4 February 2005
Abstract
Proteins can become modified by a large number of reactions involving reactive oxygen species. Among these reactions, carbonylation has attracted a great deal of attention due to its irreversible and unrepairable nature. Carbonylated proteins are marked for proteolysis by the proteasome and the Lon protease but can escape degradation and form high-molecular-weight aggregates that accumulate with age. Such carbonylated aggregates can become cytotoxic and have been associated with a large number of age-related disorders, including Parkinson's disease, Alzheimer's disease, and cancer. This review focuses on the generation of and defence against protein carbonyls and speculates on the potential role of carbonylation in protein quality control, cellular deterioration, and senescence.
Keywords:
- damage segregation,
- mistranslation,
- protein carbonylation,
- proteolysis,
- senescence
