Phosphorylation of p300 by ATM controls the stability of NBS1 |
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Authors: | Eun Ryoung Jang Jae Duk Choi Gajin Jeong |
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Affiliation: | a Department of Molecular Science and Technology, College of Natural Sciences, Ajou University, Suwon 443-749, Republic of Korea b School of Biological Sciences, Seoul National University, Seoul 151, Republic of Korea |
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Abstract: | Acetyltransferase, p300 is a transcriptional cofactor of signal-responsive transcriptional regulation. The surveillance kinase ataxia-telangiectasia mutated (ATM) plays a central role in regulation of a wide range of cellular DNA damage responses. Here, we investigated whether and how ATM mediates phosphorylation of p300 in response to DNA damage and how p300 phosphorylation is functionally linked to DNA damage. ATM-phosphorylated p300 in vitro and in vivo, in response to DNA damage. Phosphorylation of p300 proteins was observed upon γ-irradiation in ATM+ cells but not ATM− cells. Importantly, expression of nonphosphorylatable serine to alanine form of p300 (S106A) destabilized both p300 and NBS1 proteins, after DNA damage. These data demonstrate that ATM transduces a DNA damage signal to p300, and that ATM-dependent phosphorylation of p300 is required for stabilization of NBS1 proteins in response to DNA damage. |
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Keywords: | p300 ATM NBS1 DNA damage |
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