Nature Communications (Aug 2020)
OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity
- Fangzhou Li,
- Qianqian Sun,
- Kun Liu,
- Ling Zhang,
- Ning Lin,
- Kaiqiang You,
- Mingwei Liu,
- Ning Kon,
- Feng Tian,
- Zebin Mao,
- Tingting Li,
- Tanjun Tong,
- Jun Qin,
- Wei Gu,
- Dawei Li,
- Wenhui Zhao
Affiliations
- Fangzhou Li
- Department of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center
- Qianqian Sun
- Department of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center
- Kun Liu
- Department of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center
- Ling Zhang
- Center for Translational Medicine, The Affiliated Zhangjiagang Hospital of Soochow University
- Ning Lin
- Department of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center
- Kaiqiang You
- Department of Biomedical informatics, School of Basic Medical Sciences, Beijing Key Laboratory of Protein Post-translational Modifications and Cell Function, Peking University Health Science Center
- Mingwei Liu
- State Key Laboratory of Proteomics, Beijing Proteome Research Center
- Ning Kon
- Institute for Cancer Genetics, and Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia University
- Feng Tian
- Department of Laboratory Animal Science, Peking University Health Science Center
- Zebin Mao
- Department of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center
- Tingting Li
- Department of Biomedical informatics, School of Basic Medical Sciences, Beijing Key Laboratory of Protein Post-translational Modifications and Cell Function, Peking University Health Science Center
- Tanjun Tong
- Department of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center
- Jun Qin
- State Key Laboratory of Proteomics, Beijing Proteome Research Center
- Wei Gu
- Institute for Cancer Genetics, and Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia University
- Dawei Li
- Center for Translational Medicine, The Affiliated Zhangjiagang Hospital of Soochow University
- Wenhui Zhao
- Department of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center
- DOI
- https://doi.org/10.1038/s41467-020-17926-7
- Journal volume & issue
-
Vol. 11,
no. 1
pp. 1 – 16
Abstract
The mechanisms by which deubiquitinases modulate tumour progression are not fully understood. Here, the authors perform an RNAi screen and identify that the deubiquitinase OTUD5 suppresses cancer growth in a TRIM25 dependent manner, which in turn controls the expression of tumour suppressor protein, PML.
