USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization

Shangda Yang, Ling Liu, Cheng Cao, Nan Song, Yuejiao Wang, Shuai Ma, Qi Zhang, Na Yu, Xiang Ding, Fuquan Yang, Shanshan Tian, Kai Zhang, Tao Sun, Jie Yang, Zhi Yao, Shaoyuan Wu and Lei Shi ()
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Shangda Yang: Tianjin Medical University
Ling Liu: Tianjin Medical University
Cheng Cao: Tianjin Medical University
Nan Song: Tianjin Medical University
Yuejiao Wang: Tianjin Medical University
Shuai Ma: Tianjin Medical University
Qi Zhang: Tianjin Medical University
Na Yu: Tianjin Medical University
Xiang Ding: Chinese Academy of Sciences
Fuquan Yang: Chinese Academy of Sciences
Shanshan Tian: Tianjin Medical University
Kai Zhang: Tianjin Medical University
Tao Sun: Nankai University
Jie Yang: Tianjin Medical University
Zhi Yao: Tianjin Medical University
Shaoyuan Wu: Tianjin Medical University
Lei Shi: Tianjin Medical University

Nature Communications, 2018, vol. 9, issue 1, 1-17

Abstract: Abstract Histone chaperone ASF1A has been reported to be dysregulated in multiple tumors; however, the underlying molecular mechanism that how the abundance and function of ASF1A are regulated remains unclear. Here we report that ASF1A is physically associated with USP52, which is previously identified as a pseudo-deubiquitinase. Interestingly, we demonstrate that USP52 is a bona fide ubiquitin-specific protease, and USP52 promotes ASF1A deubiquitination and stabilization. USP52-promoted ASF1A stabilization facilitates chromatin assembly and favors cell cycle progression. Additionally, we find that USP52 is overexpressed in breast carcinomas, and its level of expression correlates with that of ASF1A. Moreover, we reveal that impairment of USP52-promoted ASF1A stabilization results in growth arrest of breast cancer cells and sensitizes these cells to DNA damage. Our experiments identify USP52 as a truly protein deubiquitinase, uncover a molecular mechanism of USP52 in chromatin assembly, and reveal a potential role of USP52 in breast carcinogenesis.

Date: 2018
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DOI: 10.1038/s41467-018-03588-z

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