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Pellino1 regulates reversible ATM activation via NBS1 ubiquitination at DNA double-strand breaks

  • Geun Hyoung Ha
  • , Jae Hoon Ji
  • , Sunyoung Chae
  • , Jihyun Park
  • , Suhyeon Kim
  • , Jin Kwan Lee
  • , Yonghyeon Kim
  • , Sunwoo Min
  • , Jeong Min Park
  • , Tae Hong Kang
  • , Ho Lee
  • , Hyeseong Cho
  • , Chang Woo Lee

Research output: Contribution to journal › Article › peer-review

Abstract

DNA double-strand break (DSB) signaling and repair are critical for genome integrity. They rely on highly coordinated processes including posttranslational modifications of proteins. Here we show that Pellino1 (Peli1) is a DSB-responsive ubiquitin ligase required for the accumulation of DNA damage response proteins and efficient homologous recombination (HR) repair. Peli1 is activated by ATM-mediated phosphorylation. It is recruited to DSB sites in ATM- and γH2AX-dependent manners. Interaction of Peli1 with phosphorylated histone H2AX enables it to bind to and mediate the formation of K63-linked ubiquitination of NBS1, which subsequently results in feedback activation of ATM and promotes HR repair. Collectively, these results provide a DSB-responsive factor underlying the connection between ATM kinase and DSB-induced ubiquitination.

Original languageEnglish (US)
Article number1577
JournalNature communications
Volume10
Issue number1
DOIs
StatePublished - Dec 1 2019
Externally publishedYes

ASJC Scopus subject areas

  • General Chemistry
  • General Biochemistry, Genetics and Molecular Biology
  • General
  • General Physics and Astronomy

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