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Significance It has been known for some time that ATM and RAD3-related kinase (ATR) phosphorylates and activates checkpoint kinase 1 (CHK1) in response to DNA damage. However, how CHK1 is targeted to chromatin and how it is released has not been fully deciphered. Previously we demonstrated that CHK1 K63-linked ubiquitination contributes to its chromatin association and activation. The study presented here highlights the involvement of ubiquitin-specific protease 3 (USP3) in removing the K63-linked ubiquitin chain, thus allowing not only the release of CHK1 from chromatin but also the access of its substrates. Together our studies have revealed a stepwise regulation of CHK1 in DNA damage response.

Deubiquitinating enzyme USP3 controls CHK1 chromatin association and activation