Interaction of The Checkpoint Protein Rad9 and The Non-homologous End-joining Protein Ku70
DOI:
Author:
Affiliation:

Key Laboratory for Protein and Peptide Pharmaceuticals, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, University of Chinese Academy of Sciences,Key Laboratory for Protein and Peptide Pharmaceuticals, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, University of Chinese Academy of Sciences,Key Laboratory for Protein and Peptide Pharmaceuticals, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, University of Chinese Academy of Sciences,Key Laboratory for Protein and Peptide Pharmaceuticals, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, University of Chinese Academy of Sciences,Key Laboratory for Protein and Peptide Pharmaceuticals, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences,Key Laboratory for Protein and Peptide Pharmaceuticals, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences,Key Laboratory for Protein and Peptide Pharmaceuticals, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences,Key Laboratory for Protein and Peptide Pharmaceuticals, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences

Clc Number:

Fund Project:

This work was supported by grants from The National Natural Science Foundation of China (31370792, U1738112)

  • Article
  • |
  • Figures
  • |
  • Metrics
  • |
  • Reference
  • |
  • Related
  • |
  • Cited by
  • |
  • Materials
  • |
  • Comments
    Abstract:

    Rad9 plays roles in both cell cycle checkpoint control and DNA repair. It can interact with the components of multiple DNA repair pathways and regulate their functions. Non-homologous end-joining (NHEJ) repair pathway is predominantly used in vertebrates for the repair of DNA double strand break (DSB). Proper activation of DNA-dependent protein kinase (DNA-PK), composed of Ku70, Ku80, and DNA-dependent protein kinase catalytic subunit (DNA-PKcs), is essential for NHEJ repair. In this study, we found that Rad9 interacts with Ku70 physically and functionally. Deletion of Rad9 gene, knockdown of Rad9 expression or removal of Rad9 protein led to inefficient DNA end-joining repair. Furthermore, loss of Rad9 impaired the DNA damage-induced binding of Ku70 to the chromatin and attenuated the DNA damage-induced kinase activity of DNA-PKcs. Taken together, our data unveil a novel functional interplay between Rad9 and the NHEJ protein Ku70, indicating a role of Rad9 in NHEJ repair through modulating the activation of the DNA-PKcs/Ku70/Ku80 complex.

    Reference
    Related
    Cited by
Get Citation

FAN Ying-Jun, LIU Yu-Heng, WANG Yu-Lan, KONG Bing-Jie, ZHAO Yun, YE Chen, AN Li-Li, HANG Hai-Ying. Interaction of The Checkpoint Protein Rad9 and The Non-homologous End-joining Protein Ku70[J]. Progress in Biochemistry and Biophysics,2018,45(10):1054-1067

Copy
Share
Article Metrics
  • Abstract:
  • PDF:
  • HTML:
  • Cited by:
History
  • Received:June 11,2018
  • Revised:August 16,2018
  • Accepted:August 29,2018
  • Online: October 22,2018
  • Published: October 20,2018