Background: Rad17 is a key DNA damage response protein that undergoes ubiquitylation-mediated degradation. Results: USP20 is a deubiquitylase that interacts with and stabilizes Rad17 in a proteasome-dependent manner, and it is required for Chk1 phosphorylation. Conclusion: USP20 is a novel regulator of the DNA damage response. Significance: USP20 role sheds more light on the ubiquitylation events associated with DNA damage, and may predict chemotherapy response.
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