Evidence map›Paper›PMID 31822558›Full record

ArticleThe Journal of biological chemistry2020

The deubiquitinase USP7 stabilizes Maf proteins to promote myeloma cell survival.

Yuanming He, Siyu Wang, Jiefei Tong, Shuoyi Jiang, Ye Yang, Zubin Zhang, Yujia Xu, Yuanying Zeng, Biyin Cao, Michael F Moran and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 60 citations in OpenAlex.

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  9. Deubiquitylating Enzymes in Cancer and Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  10. International journal of molecular sciences · 2023
    Article
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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 4 institutions in 2 countries.

Yuanming HeDepartment of Pharmacology, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu 215123, China; Guangzhou and Guangdong Key Laboratory of Protein Modification and Degradation, School of Basic Medical Sciences, Guangzhou Medical University, Xinzao Town, Panyu District, Guangzhou 511436, China.
Siyu WangDepartment of Pharmacology, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu 215123, China.
Jiefei TongProgram in Cell Biology, Hospital for Sick Children, Department of Molecular Genetics, University of Toronto, Toronto M5G 0A4, Canada.
Shuoyi JiangDepartment of Pharmacology, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu 215123, China; Guangzhou and Guangdong Key Laboratory of Protein Modification and Degradation, School of Basic Medical Sciences, Guangzhou Medical University, Xinzao Town, Panyu District, Guangzhou 511436, China.
Ye YangSchool of Basic Medicine, Nanjing University of Traditional Medicine, Nanjing 210023, China.
Zubin ZhangDepartment of Pharmacology, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu 215123, China.
Yujia XuDepartment of Pharmacology, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu 215123, China.
Yuanying ZengDepartment of Oncology, Suzhou Municipal Hospital, Suzhou 215100, China. Electronic address: zengyuanying@163.com.
Biyin CaoDepartment of Pharmacology, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu 215123, China. Electronic address: caobiyin@suda.edu.cn.
Michael F MoranProgram in Cell Biology, Hospital for Sick Children, Department of Molecular Genetics, University of Toronto, Toronto M5G 0A4, Canada.
Xinliang MaoDepartment of Pharmacology, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu 215123, China; Guangzhou and Guangdong Key Laboratory of Protein Modification and Degradation, School of Basic Medical Sciences, Guangzhou Medical University, Xinzao Town, Panyu District, Guangzhou 511436, China; Guangzhou Institute of Cardiovascular Disease and Department of Hematology, the Second Affiliated Hospital, Guangzhou Medical University, Guangzhou 510260, China. Electronic address: xinliangmao@suda.edu.cn.
Soochow University · CNHospital for Sick Children · CASuzhou Municipal Hospital · CNUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Maf proteins, including c-Maf, MafA, and MafB, are critical transcription factors in myelomagenesis. Previous studies demonstrated that Maf proteins are processed by the ubiquitin-proteasome pathway, but the mechanisms remain elusive. This study applied MS to identify MafB ubiquitination-associated proteins and found that the ubiquitin-specific protease USP7 was present in the MafB interactome. Moreover, USP7 also interacted with c-Maf and MafA and blocked their polyubiquitination and degradation. Consistently, knockdown of USP7 resulted in Maf protein degradation along with increased polyubiquitination levels. The action of USP7 thus promoted Maf transcriptional activity as evidenced by luciferase assays and by the up-regulation of the expression of Maf-modulated genes. Furthermore, USP7 was up-regulated in myeloma cells, and it was negatively associated with the survival of myeloma patients. USP7 promoted myeloma cell survival, and when it was inhibited by its specific inhibitor P5091, myeloma cell lines underwent apoptosis. These results therefore demonstrated that USP7 is a deubiquitinase of Maf proteins and promotes MM cell survival in association with Maf stability. Given the significance of USP7 and Maf proteins in myeloma genesis, targeting the USP7/Maf axle is a potential strategy to the precision therapy of MM.

Indexed as

ApoptosisCarcinogenesisCell ProliferationCell SurvivalFemaleGene Expression Regulation, NeoplasticHEK293 CellsHumansMafB Transcription FactorMaf Transcription Factors, LargeMaleMultiple MyelomaPolyubiquitinProgression-Free SurvivalProteolysisProto-Oncogene Proteins c-mafMAFA protein, humanMAFB protein, humanMafB Transcription FactorMAF protein, humanMaf Transcription Factors, LargeP5091PolyubiquitinProto-Oncogene Proteins c-mafThiophenesUbiquitin-Specific Peptidase 7USP7 protein, humananticancer drugcancerdeubiquitylation (deubiquitination)multiple myelomatranscription factor

Identifiers

PMID31822558
PMCPMC7029123
OpenAlexW2996110664

What OpenQuestion holds

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Registered trials

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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.