Lysine-specific modifications of p53: a matter of life and death?
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Diana Marouco1, Alexander V. Garabadgiu2, Gerry Melino2,3,4 and Nikolai A. Barlev1,2,5
1 Department of Biochemistry, University of Leicester, Leicester, UK;
2 Molecular Pharmacology Laboratory, Saint-Petersburg Institute of Technology, Saint-Petersburg, Russia;
3 MRC Toxicology Unit, University of Leicester, Leicester, UK;
4 Faculty of Medicine, University of Rome “Tor Vergata”, Rome, Italy
5 Gene Expression Laboratory, Institute of Cytology, Saint-Petersburg, Russia
Nikolai A. Barlev, email:
Keywords: p53, post-translational modifications, lysine methylation, acetylation
Received: September 23, 2013 Accepted: October 5, 2013 Published: October 8, 2013
Post-translational modifications provide a fine-tuned control of protein function(s) in the cell. The well-known tumour suppressor p53 is subject to many post-translational modifications, which alter its activity, localization and stability, thus ultimately modulating its response to various forms of genotoxic stress. In this review, we focus on the role of recently discovered lysine-specific modifications of p53, methylation and acetylation in particular, and their effects on p53 activity in damaged cells. We also discuss a possibility of mutual influence of covalent modifications in the p53 and histone proteins located in the vicinity of p53 binding sites in chromatin and propose important ramifications stemming from this hypothesis.
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