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.
Department of Integration of Chinese and Western Medicine, School of Basic Medical Sciences, Peking University Health Science Center, Beijing 100191, China.
Nucleic Acids Res. 2019 Oct 10;47(18):9721-9740. doi: 10.1093/nar/gkz726.
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.
组蛋白动态如何受到调控以确保有效的 DNA 修复仍然有待理解。在这里，我们报告了泛素特异性蛋白酶 USP11 作为一种组蛋白去泛素化酶来催化 H2AK119 和 H2BK120 的去泛素化。我们表明，USP11 与染色质重塑 NuRD 复合物在物理上相关，并在 DNA 修复过程中发挥功能。我们证明了 USP11 介导的组蛋白去泛素化和 NuRD 相关的组蛋白去乙酰化协调作用，以允许及时终止 DNA 修复和染色质结构的重组。因此，USP11 参与染色质浓缩、基因组稳定性和细胞存活。总之，这些观察结果表明，USP11 是一种染色质修饰物，它在 DNA 损伤反应和基因组稳定性的维持中起着至关重要的作用。
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