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USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization

Author

Listed:
  • 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
    Tianjin Medical University)

  • Zhi Yao

    (Tianjin Medical University)

  • Shaoyuan Wu

    (Tianjin Medical University)

  • Lei Shi

    (Tianjin Medical University
    Tianjin Medical University)

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.

Suggested Citation

  • 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 & Lei Sh, 2018. "USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization," Nature Communications, Nature, vol. 9(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03588-z
    DOI: 10.1038/s41467-018-03588-z
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    Cited by:

    1. Sumin Feng & Sai Ma & Kejiao Li & Shengxian Gao & Shaokai Ning & Jinfeng Shang & Ruiyuan Guo & Yingying Chen & Britny Blumenfeld & Itamar Simon & Qing Li & Rong Guo & Dongyi Xu, 2022. "RIF1-ASF1-mediated high-order chromatin structure safeguards genome integrity," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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