Acetylation and phosphorylation of the carboxy-terminal domain of p53: regulative significance

Oncol Res. 1998;10(2):55-7. Acetylation and phosphorylation of the carboxy-terminal domain of p53: regulative significance. Chiarugi V, Cinelli M, Magnelli L. Source Laboratory of Molecular Biology, University of Florence, Italy. Abstract Three fundamental domains are conventionally distinguished on the p53 molecule: an NH2 domain involved in transcription, a central core domain involved in specific DNA binding to the consensus sequences, and a carboxy-terminal domain of about 30 amino acids working as a basic regulatory domain, exhibiting aspecific DNA binding, tetramerization, and nuclearization. The presence of an unmodified carboxy-terminus does not allow the specific transactivation transcriptional function of the p53 protein. Therefore, for the activation of the protein function the carboxy-terminus must be modified. In the present commentary we discuss the role of two covalent modification events occurring at the carboxy-terminus, namely phosphorylation and acetylation, as well as the specific role of these events in the functional regulation of p53 molecule. PMID: 9666512 [PubMed - indexed for MEDLINE]