Evidence map›Paper›PMID 28042509›Full record

ArticleAmerican journal of cancer research2016

Ubiquitin-specific protease 11 (USP11) functions as a tumor suppressor through deubiquitinating and stabilizing VGLL4 protein.

Encheng Zhang, Bing Shen, Xingyu Mu, Yan Qin, Fang Zhang, Yong Liu, Jiantao Xiao, Pingzhao Zhang, Chenji Wang, Mingyue Tan and 1 more

Open access · greenAbstract read
In one paragraph

Article in American journal of cancer research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Deubiquitylating Enzymes in Cancer and Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  8. Article
  9. Review
  10. Article
  11. The Dual Role of USP11 in Cancer.Journal of oncology · 2022
    Review
  12. Article
  13. Review
  14. Article
  15. The role of deubiquitinating enzymes in cancer drug resistance.Cancer chemotherapy and pharmacology · 2020
    Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. TGF-β signaling pathway mediated by deubiquitinating enzymes.Cellular and molecular life sciences : CMLS · 2019
    Review
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 2 institutions in 1 country.

Encheng ZhangDepartment of Urology, Shanghai General Hospital, School of Medicine, Shanghai Jiaotong University Shanghai, P. R. China.
Bing ShenDepartment of Urology, Shanghai General Hospital, School of Medicine, Shanghai Jiaotong University Shanghai, P. R. China.
Xingyu MuDepartment of Urology, Shanghai General Hospital, School of Medicine, Shanghai Jiaotong University Shanghai, P. R. China.
Yan QinDepartment of Urology, Shanghai General Hospital, School of Medicine, Shanghai Jiaotong University Shanghai, P. R. China.
Fang ZhangDepartment of Urology, Shanghai General Hospital, School of Medicine, Shanghai Jiaotong University Shanghai, P. R. China.
Yong LiuDepartment of Urology, Shanghai General Hospital, School of Medicine, Shanghai Jiaotong University Shanghai, P. R. China.
Jiantao XiaoDepartment of Urology, Shanghai General Hospital, School of Medicine, Shanghai Jiaotong University Shanghai, P. R. China.
Pingzhao ZhangState Key Laboratory of Genetic Engineering, Collaborative Innovation Center for Genetics and Development, School of Life Sciences, Fudan University Shanghai, P. R. China.
Chenji WangState Key Laboratory of Genetic Engineering, Collaborative Innovation Center for Genetics and Development, School of Life Sciences, Fudan University Shanghai, P. R. China.
Mingyue TanDepartment of Urology, Shanghai General Hospital, School of Medicine, Shanghai Jiaotong University Shanghai, P. R. China.
Yu FanDepartment of Urology, Shanghai General Hospital, School of Medicine, Shanghai Jiaotong University Shanghai, P. R. China.
Shanghai Jiao Tong University · CNFudan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

VGLL4 is a transcriptional repressor that interacts with transcription factors TEADs and inhibits YAP-induced overgrowth and tumorigenesis. VGLL4 protein was dramatically reduced in various types of human cancers. But how VGLL4 protein is post-transcriptional regulated is poorly understood. In this study, we identify deubiquitinating enzyme USP11 as a novel VGLL4 interactor. We reveal that the USP domain of USP11 and the N-terminal region of VGLL4 are required for mutual binding. USP11 controls VGLL4 protein stability by promoting its deubiquitination. Furthermore, our results show that knockdown of USP11 promotes cell growth, migration, and invasion in a YAP-dependent manner. Together, our results suggest that USP11 may exert its tumor suppressor role by modulating VGLL4/YAP-TEADs regulatory loop.

Indexed as

deubiquitinationHippo pathwayTEADsUSP11VGLL4

Identifiers

PMID28042509
PMCPMC5199763
OpenAlexW2602362410

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.