Evidence map›Paper›PMID 29992764›Full record

ArticleCancer medicine2018

Deubiquitination and stabilization of programmed cell death ligand 1 by ubiquitin-specific peptidase 9, X-linked in oral squamous cell carcinoma.

Wu Jingjing, Guo Wenzheng, Wen Donghua, Hou Guangyu, Zhou Aiping, Wu Wenjuan

Open access · goldAbstract read
In one paragraph

Article in Cancer medicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed, 1 pooled it
2.6field-weighted citation impact, top 7% 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

60 citing papers in PubMed, 1 synthesis or guideline pooled it, 79 citations in OpenAlex.

  1. Pooled it
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  6. Proteostasis of immune checkpoint receptors.The Biochemical journal · 2025
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  12. Deubiquitinases and Cancer.Journal of pharmacy & bioallied sciences · 2024
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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

6 authors at 3 institutions in 2 countries.

Wu JingjingDepartment of Laboratory Medicine, Shanghai East Hospital, Tongji University School of Medicine, Shanghai, China.ORCID 0000-0002-6579-6738
Guo WenzhengDepartment of Laboratory Medicine, Shanghai East Hospital, Tongji University School of Medicine, Shanghai, China.
Wen DonghuaDepartment of Laboratory Medicine, Shanghai East Hospital, Tongji University School of Medicine, Shanghai, China.
Hou GuangyuDepartment of Oral and Maxillofacial surgery, Hospital of Stomatology, Tongji University, Shanghai, China.
Zhou AipingDepartment of Laboratory Medicine, Shanghai East Hospital, Tongji University School of Medicine, Shanghai, China.
Wu WenjuanDepartment of Laboratory Medicine, Shanghai East Hospital, Tongji University School of Medicine, Shanghai, China.
Shanghai East Hospital · CNShanghai Jiao Tong University · CNTongji University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe immune checkpoint protein programmed cell death ligand 1 (PD-L1) binds to PD1 to promote tumor cell escape from the killing effect of the immune system. However, there are few studies on the regulatory mechanisms of PD-L1 in tumors. Although PD-L1 has been reported to undergo ubiquitination in some cancers, its regulatory mechanisms in oral squamous cell carcinoma (OSCC) are unclear. Therefore, we aimed to investigate this phenomenon.

methodsWe examined the expression and function of USP9X and PD-L1 in human oral keratinocytes (HOK) and OSCC cell lines (HN4 and HN30) as the control and relevant cancer cells using western blotting, immunoprecipitation, immunohistochemistry (IHC), T-cell-mediated tumor cell killing assay, and liquid chromatography-mass spectrometry.

resultsProgrammed cell death ligand 1 was highly expressed in OSCC by the regulation of the ubiquitin-proteasome pathway. Furthermore, we discovered that ubiquitin-specific peptidase 9, X-linked (USP9X) could be combined with PD-L1 to induce its deubiquitination and stabilize its protein expression in OSCC.

conclusionOur data indicate that USP9X deubiquitinates and stabilizes PD-L1. Suppressing the expression of USP9X blocks tumor cell growth. The results provide a theoretical basis for USP9X as a therapeutic target.

Indexed as

B7-H1 AntigenBiomarkersCarcinoma, Squamous CellGene ExpressionHumansKeratinocytesMouth NeoplasmsProtein BindingProtein StabilityUbiquitinationUbiquitin ThiolesteraseB7-H1 AntigenBiomarkersCD274 protein, humanUbiquitin ThiolesteraseUSP9X protein, humanoral squamous cell carcinomaprogrammed cell death ligand 1programmed cell death protein 1ubiquitin-specific peptidase 9, X-linked

Identifiers

PMID29992764
PMCPMC6089178
OpenAlexW2814902257

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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.