Lysine-specific modifications of p53: A matter of life and death?

Diana Marouco, Alexander V. Garabadgiu, Gerry Melino, Nikolai A. Barlev

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)1556-1571
Number of pages16
Issue number10
Publication statusPublished - Oct 2013


  • Acetylation
  • Lysine methylation
  • p53
  • Post-translational modifications

ASJC Scopus subject areas

  • Oncology


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