Evidence map›Paper›PMID 33531626›Full record

ArticleOncogene2021

The deubiquitinase USP11 regulates cell proliferation and ferroptotic cell death via stabilization of NRF2 USP11 deubiquitinates and stabilizes NRF2.

Chunjie Meng, Jun Zhan, Delin Chen, Genze Shao, Hongquan Zhang, Wei Gu, Jianyuan Luo

Abstract read
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In one paragraph

Article in Oncogene, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
–field-weighted citation impact
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

61 citing papers in PubMed.

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  10. Okanin Suppresses the Growth of Colorectal Cancer Cells by Targeting at Peroxiredoxin 5.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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1 more citing papers are in PubMed but not listed here.

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

7 authors.

Chunjie Meng *Department of Medical Genetics, Department of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Center for Medical Genetics, Peking University Health Science Center, Beijing, China.
Jun Zhan *Department of Human Anatomy, Histology, and Embryology, Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education) and State Key Laboratory of Natural and Biomimetic Drugs, Peking University Health Science Center, Beijing, China.
Delin ChenInstitute for Cancer Genetics, Department of Pathology and Cell Biology, Columbia University, New York, NY, USA.
Genze ShaoDepartment of Cell Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.ORCID http://orcid.org/0000-0002-4374-3969
Hongquan ZhangDepartment of Human Anatomy, Histology, and Embryology, Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education) and State Key Laboratory of Natural and Biomimetic Drugs, Peking University Health Science Center, Beijing, China.
Wei GuInstitute for Cancer Genetics, Department of Pathology and Cell Biology, Columbia University, New York, NY, USA.ORCID http://orcid.org/0000-0002-1480-2368
Jianyuan LuoDepartment of Medical Genetics, Department of Biochemistry and Biophysics, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Center for Medical Genetics, Peking University Health Science Center, Beijing, China. luojianyuan@bjmu.edu.cn.ORCID http://orcid.org/0000-0001-6057-2914

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transcription factor nuclear factor (erythroid-derived 2)-like 2 (NRF2) plays a key role in cancer progression and is tightly regulated by the proteasome pathway. E3 ligases that mediate NRF2 ubiquitination have been widely reported, but the mechanism of NRF2 deubiquitination remains largely unclear. Here, we identified ubiquitin-specific-processing protease 11 (USP11) in NRF2 complexes and confirmed an interaction between these two proteins. We further found that USP11 deubiquitinates NRF2; this modification stabilizes NRF2. Functionally, USP11 depletion contributes to the suppression of cell proliferation and induction of ferroptotic cell death due to ROS-mediated stress, which can be largely abrogated by overexpression of NRF2. Finally, immunohistochemical staining of USP11 and NRF2 was performed using a lung tissue microarray, which revealed that USP11 is highly expressed in patients with NSCLC and positively correlated with NRF2 expression. Together, USP11 stabilizes NRF2 and is thus an important player in cell proliferation and ferroptosis.

Indexed as

Carcinoma, Non-Small-Cell LungCell NucleusCell ProliferationDeubiquitinating EnzymesHumansNF-E2-Related Factor 2Oxidative StressProteasome Endopeptidase ComplexReactive Oxygen SpeciesSignal TransductionThiolester HydrolasesUbiquitinationUbiquitin-Protein LigasesDeubiquitinating EnzymesNFE2L2 protein, humanNF-E2-Related Factor 2Proteasome Endopeptidase ComplexReactive Oxygen SpeciesThiolester HydrolasesUbiquitin-Protein LigasesUSP11 protein, human

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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.