Journal
EMBO REPORTS
Volume 7, Issue 2, Pages 192-198Publisher
WILEY
DOI: 10.1038/sj.embor.7400591
Keywords
Rb; E2F; acetylation; DNA damage
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Funding
- Cancer Research UK [13058] Funding Source: Medline
- Medical Research Council [G9400953, G0500905] Funding Source: Medline
- MRC [G9400953, G0500905] Funding Source: UKRI
- Medical Research Council [G0500905, G9400953] Funding Source: researchfish
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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.
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