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Nucleic Acids Res. 2019 Oct 10;47(18):9721-9740. doi: 10.1093/nar/gkz726.

USP11 acts as a histone deubiquitinase functioning in chromatin reorganization during DNA repair.

Ting X1, Xia L1, Yang J1,2, He L1,3, Si W4, Shang Y1,3, Sun L1,2.

Author information

1
Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China.
2
Department of Integration of Chinese and Western Medicine, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China.
3
Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Capital Medical University, Beijing 100069, China.
4
Department of Laboratory Medicine, Peking University Third Hospital, Beijing 100191, China.

Abstract

How chromatin dynamics is regulated to ensure efficient DNA repair remains to be understood. Here, we report that the ubiquitin-specific protease USP11 acts as a histone deubiquitinase to catalyze H2AK119 and H2BK120 deubiquitination. We showed that USP11 is physically associated with the chromatin remodeling NuRD complex and functionally involved in DNA repair process. We demonstrated that USP11-mediated histone deubiquitination and NuRD-associated histone deacetylation coordinate to allow timely termination of DNA repair and reorganization of the chromatin structure. As such, USP11 is involved in chromatin condensation, genomic stability, and cell survival. Together, these observations indicate that USP11 is a chromatin modifier critically involved in DNA damage response and the maintenance of genomic stability.

PMID:
31504778
PMCID:
PMC6765148
DOI:
10.1093/nar/gkz726
[Indexed for MEDLINE]
Free PMC Article

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