Premium
Protein phosphatase 1γ is responsible for dephosphorylation of histone H3 at Thr 11 after DNA damage
Author(s) -
Shimada Midori,
Haruta Mayumi,
Niida Hiroyuki,
Sawamoto Kazunobu,
Nakanishi Makoto
Publication year - 2010
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2010.152
Subject(s) - dephosphorylation , dna damage , phosphorylation , histone , biology , histone h3 , phosphatase , chromatin , microbiology and biotechnology , dna repair , g2 m dna damage checkpoint , dna , biochemistry , cell cycle , gene , cell cycle checkpoint
The DNA‐damage‐induced transcriptional suppression of cell cycle regulatory genes correlates with a reduction in histone H3‐Thr 11 phosphorylation (H3‐pThr 11) on their promoters that is partly mediated by the dissociation of Chk1 from chromatin. In this study, we identify protein phosphatase 1γ (PP1γ) as a phosphatase responsible for DNA‐damage‐induced H3‐pThr 11 dephosphorylation. PP1γ is activated after DNA damage, which is mainly mediated by a reduction in Cdk‐dependent phosphorylation of PP1γ at Thr 311. The depletion of PP1γ sensitizes HCT116 cells to DNA damage. Our results suggest that the ataxia telangiectasia, mutated and Rad3‐related–Chk1 axis regulates H3‐pThr 11 dephosphorylation on DNA damage, at least in part by the activation of PP1γ through Chk1‐dependent inhibition of Cdks.