Evidence map›Paper›PMID 33328570›Full record

ArticleCell death and differentiation2021

Deubiquitinating enzyme OTUB1 promotes cancer cell immunosuppression via preventing ER-associated degradation of immune checkpoint protein PD-L1.

Dan Zhu, Ruidan Xu, Xinping Huang, Zefang Tang, Yonglu Tian, Jinfang Zhang, Xiaofeng Zheng

Open access · bronzeAbstract read
In one paragraph

Article in Cell death and differentiation, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed, 1 pooled it
7.8field-weighted citation impact, top 2% 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

128 citing papers in PubMed, 1 synthesis or guideline pooled it, 172 citations in OpenAlex.

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  20. Intracellular PD-L1: Functions, Regulation, and Therapeutic Implications.International journal of biological sciences · 2026
    Review

68 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 at 2 institutions in 1 country.

Dan ZhuState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China.
Ruidan XuState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China.ORCID http://orcid.org/0000-0002-3941-4054
Xinping HuangState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China.
Zefang TangBiomedical Pioneering Innovation Center, School of Life Sciences, Peking University, Beijing, China.
Yonglu TianKey Laboratory of Cell Proliferation and Differentiation of the Ministry of Education, State Key Laboratory of Membrane Biology, School of Life Sciences, Peking University, Beijing, China.
Jinfang ZhangFrontier Science Center for Immunology and Metabolism, Medical Research Institute, Wuhan University, Wuhan, China.
Xiaofeng ZhengState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, China. xiaofengz@pku.edu.cn.ORCID http://orcid.org/0000-0001-6790-0669
Peking University · CNWuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Upregulation of programmed death ligand 1 (PD-L1) helps tumor cells escape from immune surveillance, and therapeutic antibodies targeting PD-1/PD-L1 have shown better patient outcomes only in several types of malignancies. Recent studies suggest that the clinical efficacy of anti-PD-1/PD-L1 treatments is associated with PD-L1 levels; however, the underlying mechanism of high PD-L1 protein levels in cancers is not well defined. Here, we report that the deubiquitinase OTUB1 positively regulates PD-L1 stability and mediates cancer immune responses through the PD-1/PD-L1 axis. Mechanistically, we demonstrate that OTUB1 interacts with and removes K48-linked ubiquitin chains from the PD-L1 intracellular domain in a manner dependent on its deubiquitinase activity to hinder the degradation of PD-L1 through the ERAD pathway. Functionally, depletion of OTUB1 markedly decreases PD-L1 abundance, reduces PD-1 protein binding to the tumor cell surface, and causes increased tumor cell sensitivity to human peripheral blood mononuclear cells (PBMCs)-mediated cytotoxicity. Meanwhile, OTUB1 ablation-induced PD-L1 destabilization facilitates more CD8

Indexed as

AdultAnimalsCell Line, TumorCysteine EndopeptidasesDeubiquitinating EnzymesDisease Models, AnimalHealthy VolunteersHumansImmunosuppression TherapyImmunotherapyMiceProgrammed Cell Death 1 ReceptorTransfectionUp-RegulationYoung AdultCysteine EndopeptidasesDeubiquitinating EnzymesOtub1 protein, mouseProgrammed Cell Death 1 Receptor

Identifiers

PMID33328570
PMCPMC8184985
OpenAlexW3111780573

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.