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. © 2011 Wiley‐Liss, Inc.