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The pRb (retinoblastoma protein) tumour suppressor protein has a crucial role in regulating the G1- to S-phase transition, and its phosphorylation by cyclin-dependent kinases is an established and important mechanism in controlling pRb activity. In addition, the targeted acetylation of lysine (K) residues 873/874 in the carboxy-terminal region of pRb located within a cyclin-dependent kinase-docking site hinders pRb phosphorylation and thereby retains pRb in an active state of growth suppression. Here, we report that the acetylation of pRb K873/874 occurs in response to DNA damage and that acetylation regulates the interaction between the C-terminal E2F-1-specific domain of pRb and E2F-1. These results define a new role for pRb acetylation in the DNA damage signalling pathway, and suggest that the interaction between pRb and E2F-1 is controlled by DNA-damage-dependent acetylation of pRb.

Original publication




Journal article



Publication Date





192 - 198


Acetylation, Animals, Cell Line, Tumor, Cell Nucleus, DNA Damage, E2F1 Transcription Factor, Etoposide, Fluorescent Dyes, Gene Expression Regulation, Humans, Indoles, Luciferases, Mice, Models, Biological, NIH 3T3 Cells, Nuclear Proteins, Nucleic Acid Synthesis Inhibitors, Protein Structure, Tertiary, Retinoblastoma Protein, Transfection