Acetylation and phosphorylation of the carboxy-terminal domain of p53: regulative significance.
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.
Laboratory of Molecular Biology, University of Florence, Italy.
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V
Chiarugi
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Cinelli
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L
Magnelli
D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism; D017398:Alternative Splicing; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism; D004247:DNA / Q000378:metabolism*; D004249:DNA Damage; D004260:DNA Repair; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry / Q000378:metabolism*
D016159:Tumor Suppressor Protein p53; D004247:DNA; D000123:Acetyltransferases; D011493:Protein Kinase C; D017871:Calcium-Calmodulin-Dependent Protein Kinases