Evidence map›Paper›PMID 33074477›Full record

ArticleCellular oncology (Dordrecht, Netherlands)2021

Ubiquitin-specific protease 2a promotes hepatocellular carcinoma progression via deubiquitination and stabilization of RAB1A.

Bin Xiong, Junwei Huang, Yan Liu, Min Zou, Zhibo Zhao, Jianping Gong, Xiaoling Wu, Chan Qiu

Abstract read
In one paragraph

Article in Cellular oncology (Dordrecht, Netherlands), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 27 citations in OpenAlex.

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  6. Deubiquitylating Enzymes in Hepatocellular Carcinoma.International journal of biological sciences · 2025
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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

8 authors at 3 institutions in 1 country.

Bin Xiong *Department of Hepatobiliary Surgery, The Second Affiliated Hospital of Chongqing Medical University, Chongqing, 400010, People's Republic of China.
Junwei Huang *Department of Hepatobiliary Surgery, The Second Affiliated Hospital of Chongqing Medical University, Chongqing, 400010, People's Republic of China.
Yan LiuDepartment of Gastroenterology, The Fifth people's Hospital of Chengdu, Chengdu, Sichuan, 611130, People's Republic of China.
Min ZouDepartment of Gastroenterology, The Second Affiliated Hospital of Chongqing Medical University, Chongqing, 400010, People's Republic of China.
Zhibo ZhaoDepartment of Hepatobiliary Surgery, The Second Affiliated Hospital of Chongqing Medical University, Chongqing, 400010, People's Republic of China.
Jianping GongDepartment of Hepatobiliary Surgery, The Second Affiliated Hospital of Chongqing Medical University, Chongqing, 400010, People's Republic of China.
Xiaoling WuDepartment of Gastroenterology, The Second Affiliated Hospital of Chongqing Medical University, Chongqing, 400010, People's Republic of China.
Chan QiuDepartment of Gastroenterology, The Second Affiliated Hospital of Chongqing Medical University, Chongqing, 400010, People's Republic of China. qiuchan@stu.cqmu.edu.cn.
Chongqing Medical University · CNDalian Medical University · CNChengdu Fifth People's Hospital · CN

Funding

Natural Science Foundation of Chongqing cstc2020jcyj-msxmX0214the Science & Technology Department of Sichuan Province 2018JY0276
6 · The paper itself

Abstract

purposeDeubiquitination, the inverse process of ubiquitination, is catalyzed by deubiquitinases (DUBs) that remove ubiquitin from target proteins and subsequently prevent their degradation by proteasomes. Previously, deubiquitination has been found to be involved in hepatocellular carcinoma (HCC) progression. As yet, however, little is known about the exact role of deubiquitination in the development and/or progression of this type of cancer.

methodsHCC tissues and tissue microarrays were used to detect expression of the DUB ubiquitin-specific protease 2a (USP2a). The critical role of USP2a in HCC development and progression was assessed in both in vitro cell and in vivo animal models. LC-MS/MS analyses were performed to identify potential targets of USP2a in HCC cells, after which regulation of target protein stability and ubiquitin status by USP2a were investigated.

resultsWe found that USP2a was significantly upregulated in HCC tissues, and that a high expression was positively associated with a poor prognosis. Subsequently, we found that USP2a silencing resulted in inhibition of HCC cell proliferation, migration and invasion, whereas exogenous USP2a overexpression resulted in the opposite effects, both in vitro and in vivo. Mechanistically, LC-MS/MS analysis revealed that RAB1A, a key regulator of the ER and Golgi vesicular transport system, serves as a potential target of USP2a in HCC cells. In addition, we found that USP2a can deubiquitinate and stabilize RAB1A and prevent its degradation, and that this process is required for inducing HCC progression by USP2a.

conclusionsOur data indicate that USP2a can promote HCC progression via deubiquitination and stabilization of RAB1A. This observation indicates that DUB targeting may serve as a novel approach to improve the treatment of HCC.

Indexed as

Disease ProgressionUbiquitinationAnimalsCarcinogenesisCarcinoma, HepatocellularCell Line, TumorCell MovementCell ProliferationFemaleHumansLiver NeoplasmsLymphatic MetastasisMaleMiceMice, Inbred BALB CMice, NudeRAB1A protein, humanrab1 GTP-Binding ProteinsUbiquitin ThiolesteraseUSP2 protein, humanDeubiquitinaseHepatocellular carcinomaRAB1AUSP2a

Identifiers

PMID33074477
PMCPMC12980744
OpenAlexW3092883215

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.