Evidence map›Paper›PMID 26280536›Full record

ArticleNature cell biology2015

Deubiquitylase OTUD3 regulates PTEN stability and suppresses tumorigenesis.

Lin Yuan, Yanrong Lv, Hongchang Li, Haidong Gao, Shanshan Song, Yuan Zhang, Guichun Xing, Xiangzhen Kong, Lijing Wang, Yang Li and 7 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 papers.

0numbers the graph read from it
0cells of the map it votes in
131citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

131 citing papers in PubMed, 223 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. OTU deubiquitinases in disease: roles and targeting.Trends in molecular medicine · 2026
    Review
  10. Review
  11. Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025
    Review
  12. Review
  13. Article
  14. Research progress of DUB enzyme in breast cancer.Clinical and experimental medicine · 2025
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

71 more citing papers are in PubMed but not listed here.

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

17 authors at 8 institutions in 2 countries.

Lin YuanState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Collaborative Innovation Center for Cancer Medicine, Beijing 100850, China.
Yanrong LvDepartment of General Surgery, QiLu Hospital of Shandong University, Shandong Province 250012, China.
Hongchang LiState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Collaborative Innovation Center for Cancer Medicine, Beijing 100850, China.
Haidong GaoDepartment of General Surgery, QiLu Hospital of Shandong University, Shandong Province 250012, China.
Shanshan SongState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Collaborative Innovation Center for Cancer Medicine, Beijing 100850, China.
Yuan ZhangState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Collaborative Innovation Center for Cancer Medicine, Beijing 100850, China.
Guichun XingState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Collaborative Innovation Center for Cancer Medicine, Beijing 100850, China.
Xiangzhen KongState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Collaborative Innovation Center for Cancer Medicine, Beijing 100850, China.
Lijing WangVascular Biology Research Institute, Guangdong Pharmaceutical University, Guangdong Province 510006, China.
Yang LiDepartment of Experimental Pathology, Beijing Institute of Radiation Medicine, Beijing 100850, China.
Tao ZhouInstitute of Basic Medical Sciences, China National Center of Biomedical Analysis, Beijing 100850, China.
Daming GaoKey Laboratory of Systems Biology, Innovation Center for Cell Signaling Network, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Zhi-Xiong XiaoSchool of Life Sciences, Sichuan University, Sichuan Province 610065, China.
Yuxin YinInstitute of Systems Biomedicine, Center for Systems Biology and Medicine of Aging, Peking University Health Science Center, Beijing 100191, China.
Wenyi WeiDepartment of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02115, USA.
Fuchu HeState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Collaborative Innovation Center for Cancer Medicine, Beijing 100850, China.
Lingqiang ZhangState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Collaborative Innovation Center for Cancer Medicine, Beijing 100850, China.
Beijing Proteome Research Center · CNQilu Hospital of Shandong University · CNBeth Israel Deaconess Medical Center · USCenter for Excellence in Molecular Cell Science · CNGuangdong Pharmaceutical University · CNNational Center of Biomedical Analysis · CNPeking University · CNSichuan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PTEN is one of the most frequently mutated tumour suppressors and reduction in PTEN protein stability also plays a role in tumorigenesis. Although several ubiquitin ligases for PTEN have been identified, the deubiquitylase for de-polyubiquitylation and stabilization of PTEN is less defined. Here, we report OTUD3 as a deubiquitylase of PTEN. OTUD3 interacts with, de-polyubiquitylates and stabilizes PTEN. Depletion of OTUD3 leads to the activation of Akt signalling, induction of cellular transformation and cancer metastasis. OTUD3 transgenic mice exhibit higher levels of the PTEN protein and are less prone to tumorigenesis. Reduction of OTUD3 expression, concomitant with decreased PTEN abundance, correlates with human breast cancer progression. Furthermore, we identified loss-of-function OTUD3 mutations in human cancers, which either abolish OTUD3 catalytic activity or attenuate the interaction with PTEN. These findings demonstrate that OTUD3 is an essential regulator of PTEN and that the OTUD3-PTEN signalling axis plays a critical role in tumour suppression.

Indexed as

UbiquitinationAnimalsBreast NeoplasmsCarcinogenesisCell Line, TumorFemaleHumansMice, Inbred BALB CMice, NudeMice, TransgenicMutationNeoplasm TransplantationProtein StabilityProto-Oncogene Proteins c-aktPTEN PhosphohydrolaseSignal TransductionOTUD3 protein, humanProto-Oncogene Proteins c-aktPTEN PhosphohydrolasePTEN protein, humanUbiquitin-Specific Proteases

Identifiers

PMID26280536
OpenAlexW2148390144

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.