Evidence map›Paper›PMID 32826889›Full record

ArticleNature communications2020

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 and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.8field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Research progress of DUB enzyme in breast cancer.Clinical and experimental medicine · 2025
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors at 4 institutions in 2 countries.

Fangzhou LiDepartment of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center, 38 Xueyuan Road, 100191, Beijing, China.
Qianqian SunDepartment of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center, 38 Xueyuan Road, 100191, Beijing, China.
Kun LiuDepartment of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center, 38 Xueyuan Road, 100191, Beijing, China.
Ling ZhangCenter for Translational Medicine, The Affiliated Zhangjiagang Hospital of Soochow University, 68 Jiyang West Road, 215600, Suzhou, China.
Ning LinDepartment of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center, 38 Xueyuan Road, 100191, Beijing, China.
Kaiqiang YouDepartment of Biomedical informatics, School of Basic Medical Sciences, Beijing Key Laboratory of Protein Post-translational Modifications and Cell Function, Peking University Health Science Center, 38 Xueyuan Road, 100191, Beijing, China.
Mingwei LiuState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing, China.
Ning KonInstitute for Cancer Genetics, and Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia University, 1130 St. Nicholas Avenue, New York, NY, 10032, USA.
Feng TianDepartment of Laboratory Animal Science, Peking University Health Science Center, 38 Xueyuan Road, 100191, Beijing, China.ORCID http://orcid.org/0000-0001-8601-1023
Zebin MaoDepartment of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center, 38 Xueyuan Road, 100191, Beijing, China.
Tingting LiDepartment of Biomedical informatics, School of Basic Medical Sciences, Beijing Key Laboratory of Protein Post-translational Modifications and Cell Function, Peking University Health Science Center, 38 Xueyuan Road, 100191, Beijing, China.
Tanjun TongDepartment of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center, 38 Xueyuan Road, 100191, Beijing, China.
Jun QinState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing, China.
Wei GuInstitute for Cancer Genetics, and Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia University, 1130 St. Nicholas Avenue, New York, NY, 10032, USA.
Dawei LiCenter for Translational Medicine, The Affiliated Zhangjiagang Hospital of Soochow University, 68 Jiyang West Road, 215600, Suzhou, China. daweili@suda.edu.cn.ORCID http://orcid.org/0000-0002-1094-9282
Wenhui ZhaoDepartment of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Peking University Health Science Center, 38 Xueyuan Road, 100191, Beijing, China. zhao6025729@bjmu.edu.cn.ORCID http://orcid.org/0000-0002-7703-7106
Peking University · CNBeijing Proteome Research Center · CNCancer Genetics (United States) · USSoochow University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oncogenic processes exert their greatest effect by targeting regulators of cell proliferation. Studying the mechanism underlying growth augmentation is expected to improve clinical therapies. The ovarian tumor (OTU) subfamily deubiquitinases have been implicated in the regulation of critical cell-signaling cascades, but most OTUs functions remain to be investigated. Through an unbiased RNAi screen, knockdown of OTUD5 is shown to significantly accelerate cell growth. Further investigation reveals that OTUD5 depletion leads to the enhanced transcriptional activity of TRIM25 and the inhibited expression of PML by altering the ubiquitination level of TRIM25. Importantly, OTUD5 knockdown accelerates tumor growth in a nude mouse model. OTUD5 expression is markedly downregulated in tumor tissues. The reduced OTUD5 level is associated with an aggressive phenotype and a poor clinical outcome for cancers patients. Our findings reveal a mechanism whereby OTUD5 regulates gene transcription and suppresses tumorigenesis by deubiquitinating TRIM25, providing a potential target for oncotherapy.

Indexed as

AnimalsCell Line, TumorCell ProliferationDisease Models, AnimalDNA-Binding ProteinsFemaleGene Expression Regulation, NeoplasticGene Knockdown TechniquesGenetic Predisposition to DiseaseHEK293 CellsHeterograftsHumansLung NeoplasmsMaleMiceMice, KnockoutDNA-Binding ProteinsOtud5 protein, mouseTranscription FactorsTrim25 protein, mouseUbiquitin-Specific Proteases

Identifiers

PMID32826889
PMCPMC7442798
OpenAlexW3080211533

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.