Evidence map›Paper›PMID 32973332›Full record

ArticleOncogene2020

Deubiquitinase USP29 promotes gastric cancer cell migration by cooperating with phosphatase SCP1 to stabilize Snail protein.

Wenli Qian, Qi Li, Xinglong Wu, Wenguo Li, Qiwei Li, Jie Zhang, Mengying Li, Dan Zhang, Hongxia Zhao, Xiuqun Zou and 4 more

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.8field-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

49 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
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  8. Role of Ubiquitin-regulated EMT in Cancer Metastasis and Chemoresistance.International journal of biological sciences · 2025
    Review
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  15. Review
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  17. Article
  18. Deubiquitylating Enzymes in Cancer and Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  19. Article
  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

14 authors at 3 institutions in 2 countries.

Wenli Qian *Hongqiao Institute of Medicine, Tongren Hospital/Faculty of Basic Medicine, Shanghai Jiao Tong University School of Medicine, Shanghai, 200025, China.ORCID http://orcid.org/0000-0003-2403-3328
Qi Li *Hongqiao Institute of Medicine, Tongren Hospital/Faculty of Basic Medicine, Shanghai Jiao Tong University School of Medicine, Shanghai, 200025, China.
Xinglong WuCentral Clinical Laboratory, Lanling People's Hospital, Lanling County, 277700, Shandong Province, China.
Wenguo LiShanghai Institute of Immunology, Department of Immunology and Microbiology, and the Minister of Education Key Laboratory of Cell Death and Differentiation, Shanghai Jiao Tong University School of Medicine, Shanghai, 200025, China.
Qiwei LiDepartment of Biliary-Pancreatic Surgery, Renji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai, 200127, China.
Jie ZhangHongqiao Institute of Medicine, Tongren Hospital/Faculty of Basic Medicine, Shanghai Jiao Tong University School of Medicine, Shanghai, 200025, China.
Mengying LiHongqiao Institute of Medicine, Tongren Hospital/Faculty of Basic Medicine, Shanghai Jiao Tong University School of Medicine, Shanghai, 200025, China.
Dan ZhangHongqiao Institute of Medicine, Tongren Hospital/Faculty of Basic Medicine, Shanghai Jiao Tong University School of Medicine, Shanghai, 200025, China.
Hongxia ZhaoFaculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland.
Xiuqun ZouHongqiao Institute of Medicine, Tongren Hospital/Faculty of Basic Medicine, Shanghai Jiao Tong University School of Medicine, Shanghai, 200025, China.
Hao JiaHongqiao Institute of Medicine, Tongren Hospital/Faculty of Basic Medicine, Shanghai Jiao Tong University School of Medicine, Shanghai, 200025, China.
Lingqiang ZhangState Key Laboratory of Proteomics, National Center of Protein Sciences (Beijing), Beijing Institute of Lifeomics, Beijing, 100850, China. zhanglq@nic.bmi.ac.cn.ORCID http://orcid.org/0000-0002-9795-2141
Xiao-Dong YangShanghai Institute of Immunology, Department of Immunology and Microbiology, and the Minister of Education Key Laboratory of Cell Death and Differentiation, Shanghai Jiao Tong University School of Medicine, Shanghai, 200025, China. xdyang@shsmu.edu.cn.ORCID http://orcid.org/0000-0001-6895-0713
Zhaoyuan HouHongqiao Institute of Medicine, Tongren Hospital/Faculty of Basic Medicine, Shanghai Jiao Tong University School of Medicine, Shanghai, 200025, China. houzy@sjtu.edu.cn.ORCID http://orcid.org/0000-0003-0634-2020
Shanghai Jiao Tong University · CNBeijing Proteome Research Center · CNUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Snail is a master inducer of epithelial-mesenchymal transition (EMT) and metastasis, however, Snail protein is labile and is quickly degraded through the predominate ubiquitination-mediated proteasome pathway. Deubiquitinases (DUBs) can counteract the Snail degradation process to maintain high level of Snail protein in cancer cells. In this study, we screened a cDNA library containing 79 DUBs, and discovered that a panel of DUBs consisting of USP13, USP28, USP29, USP37, OTUD6A, and DUB3 can markedly stabilize Snail protein, with USP29 displaying the strongest activity to prevent Snail degradation. Mechanistically, USP29 enhances the interaction of Snail and SCP1, resulting in simultaneous dephosphorylation and deubiquitination of Snail and thereafter cooperative prevention of Snail degradation. Biologically, ectopic expression of USP29 promotes gastric cancer cell migration, and depletion of Snail abolishes USP29-mediated cell migration; and USP29 can be induced by major EMT and metastatic inducing factors such as TGFβ, TNFα, and hypoxia. More importantly, high expression levels of Snail, USP29, and SCP1 are associated with poor survival and prognosis. Collectively, these data indicate that Snail is a crucial substrate for USP29 to promote cell migration and USP29/SCP1 complex may be new therapeutic targets to treat metastatic cancer.

Indexed as

Cell Line, TumorCell MovementDatasets as TopicEpithelial-Mesenchymal TransitionGene Expression ProfilingGene Expression Regulation, NeoplasticHEK293 CellsHumansKaplan-Meier EstimatePhosphoprotein PhosphatasesPhosphorylationPrognosisProtein BindingProtein StabilityProteolysisSnail Family Transcription FactorsCTDSP1 protein, humanPhosphoprotein PhosphatasesSNAI1 protein, humanSnail Family Transcription FactorsUbiquitin-Specific ProteasesUSP29 protein, human

Identifiers

PMID32973332
OpenAlexW3088804829

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.