Acetylation of the DNA binding domain regulates transcription-independent apoptosis by p53.

ABSTRACT: The tumor suppressor p53 induces apoptosis by altering the transcription of pro-apoptotic targets in the nucleus and by a direct, nontranscriptional role at the mitochondria. Although the post-translational modifications regulating nuclear apoptotic functions of p53 have been thoroughly characterized, little is known of how transcription-independent functions are controlled. We and others identified acetylation of the p53 DNA binding domain at lysine 120 as a critical event in apoptosis induction. Although initial studies showed that Lys-120 acetylation plays a role in p53 function in the nucleus, we report here a role for Lys-120 acetylation in transcription-independent apoptosis. We demonstrate that the Lys-120-acetylated isoform of p53 is enriched at mitochondria. The acetylation of Lys

SUBMITTER: Sykes SM 

PROVIDER: S-EPMC2740446 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature