Evidence map›Paper›PMID 30980112›Full record

ArticleCellular and molecular life sciences : CMLS2019

The deubiquitinase OTUD5 regulates Ku80 stability and non-homologous end joining.

Fangzhou Li, Qianqian Sun, Kun Liu, Haichao Han, Ning Lin, Zhongyi Cheng, Yueming Cai, Feng Tian, Zebin Mao, Tanjun Tong and 1 more

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. OTU deubiquitinases in disease: roles and targeting.Trends in molecular medicine · 2026
    Review
  3. AKT and DUBs: a bidirectional relationship.Cellular & molecular biology letters · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Role of deubiquitinating enzymes in DNA double-strand break repair.Journal of Zhejiang University. Science. B · 2021
    Review
  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

11 authors at 3 institutions in 1 country.

Fangzhou LiDepartment of Biochemistry and Molecular Biology, Peking University Health Science Center, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, 38 Xueyuan Road, Beijing, 100191, China.
Qianqian SunDepartment of Biochemistry and Molecular Biology, Peking University Health Science Center, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, 38 Xueyuan Road, Beijing, 100191, China.
Kun LiuDepartment of Biochemistry and Molecular Biology, Peking University Health Science Center, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, 38 Xueyuan Road, Beijing, 100191, China.
Haichao HanDepartment of Biochemistry and Molecular Biology, Peking University Health Science Center, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, 38 Xueyuan Road, Beijing, 100191, China.
Ning LinDepartment of Biochemistry and Molecular Biology, Peking University Health Science Center, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, 38 Xueyuan Road, Beijing, 100191, China.
Zhongyi ChengJingjie PTM BioLab, Co. Ltd, Hangzhou Economic and Technological Development Area, Hangzhou, 310018, China.
Yueming CaiRheumatic Immunology Department, Peking University Shenzhen Hospital, Shenzhen, 518035, China.
Feng TianDepartment of Laboratory Animal Science, Peking University Health Science Center, 38 Xueyuan Road, Beijing, 100191, China.
Zebin MaoDepartment of Biochemistry and Molecular Biology, Peking University Health Science Center, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, 38 Xueyuan Road, Beijing, 100191, China.
Tanjun TongDepartment of Biochemistry and Molecular Biology, Peking University Health Science Center, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, 38 Xueyuan Road, Beijing, 100191, China.
Wenhui ZhaoDepartment of Biochemistry and Molecular Biology, Peking University Health Science Center, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, 38 Xueyuan Road, Beijing, 100191, China. zhao6025729@bjmu.edu.cn.
Peking University · CNNew England Biolabs (China) · CNPeking University Shenzhen Hospital · CN

Funding

National Natural Science Foundation of China (CN) 85141044
6 · The paper itself

Abstract

The ability of cells to repair DNA double-strand breaks (DSBs) is important for maintaining genome stability and eliminating oncogenic DNA lesions. Two distinct and complementary pathways, non-homologous end joining (NHEJ) and homologous recombination (HR), are employed by mammalian cells to repair DNA DSBs. Each pathway is tightly controlled in response to increased DSBs. The Ku heterodimer has been shown to play a regulatory role in NHEJ repair. Ku80 ubiquitination contributes to the selection of a DSB repair pathway by causing the removal of Ku heterodimers from DSB sites. However, whether Ku80 deubiquitination also plays a role in regulating DSB repair is unknown. To address this question, we performed a comprehensive study of the deubiquitinase specific for Ku80, and our study showed that the deubiquitinase OTUD5 serves as an important regulator of NHEJ repair by increasing the stability of Ku80. Further studies revealed that OTUD5 depletion impaired NHEJ repair, and hence reduced overall DSB repair. Furthermore, OTUD5-depleted cells displayed excess end resection; as a result, HR repair was facilitated by OTUD5 depletion during the S/G2 phase. In summary, our study demonstrates that OTUD5 is a specific deubiquitinase for Ku80 and establishes OTUD5 as an important and positive regulator of NHEJ repair.

Indexed as

DNA End-Joining RepairCell LineDNA Breaks, Double-StrandedDNA DamageDNA RepairEndopeptidasesG2 PhaseHumansKu AutoantigenProtein StabilityS PhaseUbiquitinationEndopeptidasesKu AutoantigenOTUD5 protein, humanDeubiquitinases libraryDNA damage responseDNA lesionDUBAXRCC5

Identifiers

PMID30980112
PMCPMC11105630
OpenAlexW2938136089

What OpenQuestion holds

Textmetadata
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.