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DNA-PKcsのリジン3241と3260はゲノムの安定性と放射線抵抗性に重要である
Authors
David J. Chen
Anthony J. Davis
Masatoshi Hasegawa
Eiichiro Mori
Publication date
1 August 2016
Publisher
'Elsevier BV'
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PubMed
Abstract
DNA-dependent protein kinase (DNA-PK) is a serine/threonine kinase that plays an essential role in the repair of DNA double-strand breaks (DSBs) in the non-homologous end-joining (NHEJ) pathway. The DNA-PK holoenzyme consists of a catalytic subunit (DNA-PKcs) and DNA-binding subunit (Ku70/80, Ku). Ku is a molecular sensor for double-stranded DNA and once bound to DSB ends it recruits DNA-PKcs to the DSB site. Subsequently, DNA-PKcs is activated and heavily phosphorylated, with these phosphorylations modulating DNA-PKcs. Although phosphorylation of DNA-PKcs is well studied, other post-translational modifications of DNA-PKcs are not. In this study, we aimed to determine if acetylation of DNA-PKcs regulates DNA-PKcs-dependent DSB repair. We report that DNA-PKcs is acetylated in vivo and identified two putative acetylation sites, lysine residues 3241 and 3260. Mutating these sites to block potential acetylation results in increased radiosensitive, a slight decrease in DSB repair capacity as assessed by γH2AX resolution, and increased chromosomal aberrations, especially quadriradial chromosomes. Together, our results provide evidence that acetylation potentially regulates DNA-PKcs.博士(医学)・甲第670号・平成29年6月28日Copyright © 2016 Elsevier Inc. All rights reserved
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info:doi/10.1016%2Fj.bbrc.2016...
Last time updated on 10/01/2021
Global Institutional repository of Nara Medical University
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