OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity
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,...
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Nature Publishing Group
2020-08-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-17926-7 |
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doaj-3f5c3332490c4893b498e60e24dbc29d2021-08-22T11:41:02ZengNature Publishing GroupNature Communications2041-17232020-08-0111111610.1038/s41467-020-17926-7OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activityFangzhou Li0Qianqian Sun1Kun Liu2Ling Zhang3Ning Lin4Kaiqiang You5Mingwei Liu6Ning Kon7Feng Tian8Zebin Mao9Tingting Li10Tanjun Tong11Jun Qin12Wei Gu13Dawei Li14Wenhui Zhao15Department of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science CenterDepartment of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science CenterDepartment of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science CenterCenter for Translational Medicine, The Affiliated Zhangjiagang Hospital of Soochow UniversityDepartment of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science CenterDepartment of Biomedical informatics, School of Basic Medical Sciences, Beijing Key Laboratory of Protein Post-translational Modifications and Cell Function, Peking University Health Science CenterState Key Laboratory of Proteomics, Beijing Proteome Research CenterInstitute for Cancer Genetics, and Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia UniversityDepartment of Laboratory Animal Science, Peking University Health Science CenterDepartment of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science CenterDepartment of Biomedical informatics, School of Basic Medical Sciences, Beijing Key Laboratory of Protein Post-translational Modifications and Cell Function, Peking University Health Science CenterDepartment of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science CenterState Key Laboratory of Proteomics, Beijing Proteome Research CenterInstitute for Cancer Genetics, and Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia UniversityCenter for Translational Medicine, The Affiliated Zhangjiagang Hospital of Soochow UniversityDepartment of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science CenterThe 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.https://doi.org/10.1038/s41467-020-17926-7 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
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 |
| spellingShingle |
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 OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity Nature Communications |
| author_facet |
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 |
| author_sort |
Fangzhou Li |
| title |
OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity |
| title_short |
OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity |
| title_full |
OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity |
| title_fullStr |
OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity |
| title_full_unstemmed |
OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity |
| title_sort |
otud5 cooperates with trim25 in transcriptional regulation and tumor progression via deubiquitination activity |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2020-08-01 |
| description |
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. |
| url |
https://doi.org/10.1038/s41467-020-17926-7 |
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