Evidence map›Paper›PMID 31748695›Full record

ArticleCell death and differentiation2020

The deubiquitinase USP10 regulates KLF4 stability and suppresses lung tumorigenesis.

Xingyun Wang, Shilin Xia, Hongchang Li, Xiang Wang, Chaonan Li, Yulin Chao, Lingqiang Zhang, Chuanchun Han

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Cell death and differentiation, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

96 citing papers in PubMed, 158 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. KCTD15 Enhances Stem Cell-Like Properties and Promotes Triple-Negative Breast Cancer Progression Through KLF4/β-Catenin Signaling.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. USP10-mediated deubiquitination and activation ofActa pharmaceutica Sinica. B · 2026
    Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Xingyun Wang *Institute of Cancer Stem Cell, Dalian Medical University, Dalian, 116044, China.
Shilin Xia *Clinical Laboratory of Integrative Medicine, The First Affiliated Hospital of Dalian Medical University, Dalian, 116027, China.
Hongchang Li *State Key Laboratory of Proteomics, National Center for Protein Sciences (Beijing), Beijing Institute of Lifeomics, 100850, Beijing, China.
Xiang Wang *Institute of Cancer Stem Cell, Dalian Medical University, Dalian, 116044, China.ORCID http://orcid.org/0000-0003-3123-2827
Chaonan LiState Key Laboratory of Proteomics, National Center for Protein Sciences (Beijing), Beijing Institute of Lifeomics, 100850, Beijing, China.
Yulin ChaoInstitute of Cancer Stem Cell, Dalian Medical University, Dalian, 116044, China.
Lingqiang ZhangState Key Laboratory of Proteomics, National Center for Protein Sciences (Beijing), Beijing Institute of Lifeomics, 100850, Beijing, China. zhanglq@nic.bmi.ac.cn.
Chuanchun HanInstitute of Cancer Stem Cell, Dalian Medical University, Dalian, 116044, China. hanchuanchun@163.com.
Dalian Medical University · CNBeijing Proteome Research Center · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Krüppel-like factor 4 (KLF4), a key transcription factor, acts as a multifunctional player involved in the progression of numerous aggressive cancers. The proteasome-dependent pathway is one of the main modalities in controlling KLF4 abundance at a posttranslational level. Although some of the ubiquitin ligases have been identified, the deubiquitinases of KLF4 and the regulatory function remain unexplored. Here, by screening ubiquitin-specific proteases that may interact with KLF4, we found ubiquitin-specific peptidase 10 (USP10) as a deubiquitinating enzyme for KLF4. Forced expression of USP10 remarkably increases KLF4 protein level by blocking the latter degradation, whereas the depletion of USP10 promotes KLF4 degradation and thus enhances tumorigenesis. Loss of USP10 in mice downregulates KLF4 expression and accelerates Kras

Indexed as

A549 CellsAnimalsCarcinogenesisCarcinoma, Non-Small-Cell LungGene Expression Regulation, NeoplasticHEK293 CellsHumansKruppel-Like Factor 4Kruppel-Like Transcription FactorsLung NeoplasmsMaleMiceMice, KnockoutMice, NudeTissue Inhibitor of Metalloproteinase-3UbiquitinationKLF4 protein, humanKlf4 protein, mouseKruppel-Like Factor 4Kruppel-Like Transcription FactorsTIMP3 protein, humanTissue Inhibitor of Metalloproteinase-3Ubiquitin ThiolesteraseUSP10 protein, human

Identifiers

PMID31748695
PMCPMC7244734
OpenAlexW2990056696

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.