title: Lysine-specific modifications of p53: a matter of life and death?
abstract: 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.
authors.forename: Diana
authors.initials: D
authors.lastname: Marouco
authors.forename: Alexander V
authors.initials: AV
authors.lastname: Garabadgiu
authors.forename: Gerry
authors.initials: G
authors.lastname: Melino
authors.forename: Nikolai A
authors.initials: NA
authors.lastname: Barlev
mesh_terms: D000818:Animals; D001665:Binding Sites; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism*
chemical_list: D016159:Tumor Suppressor Protein p53; D008239:Lysine