Abstract 3079: Akt interacts and phosphorylates PHF20, a transcription factor binding to and inducing p53

Akt regulates a diverse arrays of cellular function, including apoptosis, cellular proliferation, differentiation, and metabolism. While a number of molecules have been identified as upstream regulators or downstream targets, the mechanism by which Akt regulates these cellular processes remains elusive. Here, we identified a novel transcription factor, PHF20, which binds to Akt and p53. PHF20 is an evolutionarily conserved protein. We showed that PHF20 is a transcriptional factor and transactivates p53. Furthermore, the interaction of PHF20 and p53 led to stabilize p53. Akt phosphorylates PHF20 in vitro and in vivo, which resulted in change of PHF20 nuclear localization and disassociation of p53 from PHF20 as well as decrease of p53 expression at mRNA and protein levels. In addition, knockdown of PHF20 reduces whereas ectopic expression of PHF20 increases p53 expression. These data suggest that PHF20 is a novel substrate of Akt and plays an important role in maintaining normal p53 function. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 103rd Annual Meeting of the American Association for Cancer Research; 2012 Mar 31-Apr 4; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2012;72(8 Suppl):Abstract nr 3079. doi:1538-7445.AM2012-3079