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MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining

Putzer J Hung1, Britney Johnson2, Bo-Ruei Chen3

  • 1Department of Pathology and Laboratory Medicine, Weill Cornell Medical College, New York, NY 10065, USA; Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.

Molecular Cell
|July 19, 2018
PubMed

Insights

Modulator of retrovirus infection (MRI) acts as a crucial DNA repair adaptor. It binds DNA damage response proteins, promoting non-homologous end joining (NHEJ) and is essential for embryonic development.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • The modulator of retrovirus infection (MRI), also known as CYREN, is a protein involved in DNA repair.
  • It possesses a Ku-binding motif (KBM) and an XLF-like motif (XLM).

Purpose of the Study:

  • To investigate the role of MRI in DNA double-strand break (DSB) repair.
  • To elucidate the interaction network of MRI within the DNA damage response (DDR) pathway.

Main Methods:

  • Protein interaction studies with DDR proteins (ATM, DNA-PKcs, Ku70/80, XRCC4, XLF, PAXX).
  • Analysis of MRI's role in DSB repair using mouse models and lymphocyte assays.
  • Investigation of MRI's multimeric complex formation and localization to DSBs.

Main Results:

  • MRI is intrinsically disordered and interacts with numerous DDR proteins, including kinases and classical non-homologous end joining (cNHEJ) factors.
  • MRI forms large, multimeric complexes at DSBs, enhancing the retention of DDR factors.
  • MRI deficiency, particularly with XLF, leads to embryonic lethality and impaired cNHEJ-mediated DSB repair.

Conclusions:

  • MRI functions as a critical adaptor protein in the cNHEJ pathway.
  • Its multivalent interactions with DDR factors at DSBs enhance repair efficiency.
  • MRI is essential for embryonic development and lymphocyte DNA repair.
Keywords:
CYRENDNA double-strand break repairMRIV(D)J recombinationadaptor proteinnon-homologous end joining

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