Evidence map›Paper›PMID 29788550›Full record

ArticleCancer science2018

Ubiquitin-specific protease 22 acts as an oncoprotein to maintain glioma malignancy through deubiquitinating B cell-specific Moloney murine leukemia virus integration site 1 for stabilization.

Guan-Zhong Qiu, Xiao-Yuan Mao, Yue Ma, Xing-Chun Gao, Zhen Wang, Ming-Zhu Jin, Wei Sun, Yong-Xiang Zou, Jing Lin, Hua-Lin Fu and 1 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cancer science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  6. Deubiquitylating Enzymes in Cancer and Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
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  8. Article
  9. Review
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  11. Review
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  15. Review
  16. The role of deubiquitinating enzymes in cancer drug resistance.Cancer chemotherapy and pharmacology · 2020
    Review
  17. Review
  18. Article
  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

11 authors at 5 institutions in 1 country.

Guan-Zhong QiuDepartment of Instrument Science and Engineering, Key Lab. for Thin Film and Microfabrication Technology of Ministry of Education, School of Electronic Information and Electronic Engineering, Institute of Nano Biomedicine and Engineering, Shanghai Jiao Tong University, Shanghai, China.
Xiao-Yuan MaoDepartment of Clinical Pharmacology, Xiangya Hospital, Central South University, Changsha, China.
Yue MaDepartment of Instrument Science and Engineering, Key Lab. for Thin Film and Microfabrication Technology of Ministry of Education, School of Electronic Information and Electronic Engineering, Institute of Nano Biomedicine and Engineering, Shanghai Jiao Tong University, Shanghai, China.
Xing-Chun GaoShanxi Key Laboratory of Ischemic Cardiovascular Disease, Institute of Basic Medical Medicine, Xi'an Medical University, Xi'an, China.
Zhen WangDepartment of Instrument Science and Engineering, Key Lab. for Thin Film and Microfabrication Technology of Ministry of Education, School of Electronic Information and Electronic Engineering, Institute of Nano Biomedicine and Engineering, Shanghai Jiao Tong University, Shanghai, China.
Ming-Zhu JinShanghai Jiao Tong University School of Medicine, Shanghai, China.
Wei SunDepartment of Neurosurgery, Shanghai Changzheng Hospital, Second Military Medical University, Shanghai, China.
Yong-Xiang ZouDepartment of Neurosurgery, Shanghai Changzheng Hospital, Second Military Medical University, Shanghai, China.
Jing LinDepartment of Neurosurgery, The General Hospital of Western Air Force, Chengdu, China.ORCID http://orcid.org/0000-0001-6387-6366
Hua-Lin FuDepartment of Instrument Science and Engineering, Key Lab. for Thin Film and Microfabrication Technology of Ministry of Education, School of Electronic Information and Electronic Engineering, Institute of Nano Biomedicine and Engineering, Shanghai Jiao Tong University, Shanghai, China.
Wei-Lin JinDepartment of Instrument Science and Engineering, Key Lab. for Thin Film and Microfabrication Technology of Ministry of Education, School of Electronic Information and Electronic Engineering, Institute of Nano Biomedicine and Engineering, Shanghai Jiao Tong University, Shanghai, China.ORCID http://orcid.org/0000-0001-8011-2405
Shanghai Jiao Tong University · CNSecond Military Medical University · CNAir Force General Hospital PLA · CNCentral South University · CNXi'an Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin-specific protease 22 (USP22) is a member of the "death-from-cancer" signature, which plays a key role in cancer progression. Previous evidence has shown that USP22 is overexpressed and correlates with poor prognosis in glioma. The effect and mechanism of USP22 in glioma malignancy, especially cancer stemness, remain elusive. Herein, we find USP22 is more enriched in stem-like tumorspheres than differentiated glioma cells. USP22 knockdown inhibits cancer stemness in glioma cell lines. With a cell-penetrating TAT-tag protein, B cell-specific Moloney murine leukemia virus integration site 1 (BMI1), a robust glioma stem-cell marker, is found to mediate the effect of USP22 on glioma stemness. By immunofluorescence, USP22 and BMI1 are found to share similar intranuclear expression in glioma cells. By analysis with immunohistochemistry and bioinformatics, USP22 is found to positively correlate with BMI1 at the post-translational level only rather than at the transcriptional level. By immunoprecipitation and in vivo deubiquitination assay, USP22 is found to interact with and deubiquitinate BMI1 for protein stabilization. Microarray analysis shows that USP22 and BMI1 mutually regulate a series of genes involved in glioma stemness such as POSTN, HEY2, PDGFRA and ATF3. In vivo study with nude mice confirms the role of USP22 in promoting glioma tumorigenesis by regulating BMI1. All these findings indicate USP22 as a novel deubiquitinase of BMI1 in glioma. We propose a working model of the USP22-BMI1 axis, which promotes glioma stemness and tumorigenesis through oncogenic activation. Thus, targeting USP22 might be an effective strategy to treat glioma especially in those with elevated BMI1 expression.

Indexed as

AnimalsBrain NeoplasmsCell Transformation, NeoplasticGliomaHeterograftsHumansMiceMice, SCIDOncogene ProteinsPolycomb Repressive Complex 1Thiolester HydrolasesUbiquitin ThiolesteraseBMI1 protein, humanOncogene ProteinsPolycomb Repressive Complex 1Thiolester HydrolasesUbiquitin ThiolesteraseUsp22 protein, humanBMI1cancer stemnessdeubiquitinationgliomaUSP22

Identifiers

PMID29788550
PMCPMC6029839
OpenAlexW2803681513

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.