title: Redox modulation of p53: mechanisms and functional significance.
abstract: The tumor suppressor protein p53 functions as a stress-responsive transcription factor. In response to oxidative, nitrosative, and electrophilic insults, p53 undergoes post-translational modifications, such as oxidation and covalent modification of cysteines, nitration of tyrosines, acetylation of lysines, phosphorylation of serine/threonine residues, etc. Because p53 plays a vital role in the transcriptional regulation of genes encoding proteins involved in a wide spectrum of biochemical processes including DNA repair, cell-cycle regulation, and programmed cell death, the redox-modification of p53 appears to be an important determinant of cell fate. This review highlights the redox regulation of p53 and its consequences on cellular function.
authors.affiliation: College of Pharmacy, Seoul National University, Seoul, South Korea.
authors.forename: Do-Hee
authors.initials: DH
authors.lastname: Kim
authors.forename: Joydeb Kumar
authors.initials: JK
authors.lastname: Kundu
authors.forename: Young-Joon
authors.initials: YJ
authors.lastname: Surh
mesh_terms: D017209:Apoptosis / Q000235:genetics; D002453:Cell Cycle / Q000235:genetics; D004260:DNA Repair / Q000235:genetics; D005786:Gene Expression Regulation; D006801:Humans; D008954:Models, Biological; D010084:Oxidation-Reduction; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism* / Q000502:physiology*
chemical_list: D016159:Tumor Suppressor Protein p53