DNA‐damage‐responsive acetylation of pRb regulates binding to E2F‐1
DNA‐damage‐responsive acetylation of pRb regulates binding to E2F‐1
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DOI：
10.1038/sj.embor.7400591
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发表时间：
2006-02
期刊：
影响因子：
7.7
通讯作者：
Douglas Markham;S. Munro;Judith Soloway;D. O’Connor;N. L. La Thangue
中科院分区：
文献类型：
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作者：
Douglas Markham;S. Munro;Judith Soloway;D. O’Connor;N. L. La Thangue
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.
