Abstract:
:Human C-terminal binding protein (CtBP)-interacting protein (CtIP) is a central regulator to initiate DNA end resection and homologous recombination (HR). Several studies have shown that post-translational modifications control the activity or expression of CtIP. However, it remains unclear whether and how cells restrain CtIP activity in unstressed cells and activate CtIP when needed. Here, we identify that USP52 directly interacts with and deubiquitinates CtIP, thereby promoting DNA end resection and HR. Mechanistically, USP52 removes the ubiquitination of CtIP to facilitate the phosphorylation and activation of CtIP at Thr-847. In addition, USP52 is phosphorylated by ATM at Ser-1003 after DNA damage, which enhances the catalytic activity of USP52. Furthermore, depletion of USP52 sensitizes cells to PARP inhibition in a CtIP-dependent manner in vitro and in vivo. Collectively, our findings reveal the key role of USP52 and the regulatory complexity of CtIP deubiquitination in DNA repair.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Gao M,Guo G,Huang J,Kloeber JA,Zhao F,Deng M,Tu X,Kim W,Zhou Q,Zhang C,Yin P,Luo K,Lou Zdoi
10.1038/s41467-020-19202-0subject
Has Abstractpub_date
2020-10-23 00:00:00pages
5362issue
1issn
2041-1723pii
10.1038/s41467-020-19202-0journal_volume
11pub_type
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