Evidence map›Paper›PMID 21829568›Full record

ArticlePloS one2011

The X-linked tumor suppressor TSPX interacts and promotes degradation of the hepatitis B viral protein HBx via the proteasome pathway.

Tatsuo Kido, Jing-Hsiung James Ou, Yun-Fai Chris Lau

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

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  11. Sexual dimorphism in cancer.Nature reviews. Cancer · 2016
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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

3 authors at 3 institutions in 1 country.

Tatsuo KidoDivision of Cell and Developmental Genetics, Department of Medicine, Veterans Affairs Medical Center, University of California San Francisco, San Francisco, California, United States of America.
Jing-Hsiung James Ou
Yun-Fai Chris Lau
San Francisco VA Medical Center · USUniversity of California, San Francisco · USUniversity of Southern California · US

Funding

Sex Chromosomes and Gender Disparity in HBV-Related Hepatocellular CarcinomaR21CA152589 · NCI · NORTHERN CALIFORNIA INSTITUTE/RES/EDU · PI LAU, YUN-FAI CHRIS · 2010 to 2011
$351k
Role of the Y-Located TSPY Gene in Human OncogenesisI01BX000865 · VA · VETERANS AFFAIRS MED CTR SAN FRANCISCO · PI LAU, YUN-FAI CHRIS · 2011 to 2014
–
BLRD VA I01 BX000865NCI NIH HHS R21 CA152589
6 · The paper itself

Abstract

Hepatitis B virus (HBV) infection is a major risk for hepatocellular carcinoma (HCC), and it is a serious global health problem with two billion people exposed to it worldwide. HBx, an essential factor for viral replication and a putative oncoprotein encoded by the HBV genome, has been shown to promote oncogenic properties at multiple sites in HBV-infected liver cells. The expression level of HBx closely associates with the development and progression of HCC, therefore the mechanism(s) regulating the stability of HBx is important in oncogenesis of HBV-infected cells. We demonstrate that the X-linked tumor suppressor TSPX enhances the degradation of HBx through the ubiquitin-proteasome pathway. TSPX interacts with both HBx and a proteasome 19S lid subunit RPN3 via its C-terminal acidic tail. Most importantly, over-expression of RPN3 protects HBx from, and hence acts as a negative regulator for, proteasome-dependent degradation. TSPX abrogates the RPN3-depedent stabilization of HBx, suggesting that TSPX and RPN3 act competitively in regulation of HBx stability. Since mutation and/or epigenetic repression of X-located tumor suppressor gene(s) could significantly predispose males to human cancers, our data suggest that TSPX-induced HBx degradation could play key role(s) in hepatocarcinogenesis among HBV-infected HCC patients.

Indexed as

Blotting, WesternCarcinoma, HepatocellularCells, CulturedDNA-Binding ProteinsHumansKidneyLiver NeoplasmsNuclear ProteinsProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalReverse Transcriptase Polymerase Chain ReactionRNA, MessengerRNA, Small InterferingTrans-ActivatorsUbiquitinViral Regulatory and Accessory ProteinsDNA-Binding Proteinshepatitis B virus X proteinNuclear ProteinsProteasome Endopeptidase ComplexRNA, MessengerRNA, Small InterferingTrans-ActivatorsTSPYL2 protein, humanUbiquitinViral Regulatory and Accessory Proteins

Identifiers

PMID21829568
PMCPMC3146538
OpenAlexW2085624299

What OpenQuestion holds

Textmetadata
LicenceCC0
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.