Evidence map›Paper›PMID 31533543›Full record

ArticleEmerging microbes & infections2019

Chromatin remodelling factor BAF155 protects hepatitis B virus X protein (HBx) from ubiquitin-independent proteasomal degradation.

Huijing Chen, Yi Zhang, Shuangshuang Ye, Qiong Wu, Youfen Lin, Kaiqin Sheng, Wannan Chen, Xinjian Lin, Xu Lin

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Emerging microbes & infections, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.6field-weighted citation impact, top 29% 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

13 citing papers in PubMed, 14 citations in OpenAlex.

  1. [The E3 ubiquitin ligase KLHL8 degrades HBx protein via the ubiquitin-proteasome pathway and inhibits HBV cccDNA transcription].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2026
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  12. Correction.Emerging microbes & infections · 2020
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Huijing ChenKey Laboratory of Gastrointestinal Cancer (Fujian Medical University), Ministry of Education , Fuzhou , People's Republic of China.
Yi ZhangKey Laboratory of Gastrointestinal Cancer (Fujian Medical University), Ministry of Education , Fuzhou , People's Republic of China.
Shuangshuang YeKey Laboratory of Gastrointestinal Cancer (Fujian Medical University), Ministry of Education , Fuzhou , People's Republic of China.
Qiong WuKey Laboratory of Gastrointestinal Cancer (Fujian Medical University), Ministry of Education , Fuzhou , People's Republic of China.
Youfen LinKey Laboratory of Gastrointestinal Cancer (Fujian Medical University), Ministry of Education , Fuzhou , People's Republic of China.
Kaiqin ShengKey Laboratory of Gastrointestinal Cancer (Fujian Medical University), Ministry of Education , Fuzhou , People's Republic of China.
Wannan ChenKey Laboratory of Gastrointestinal Cancer (Fujian Medical University), Ministry of Education , Fuzhou , People's Republic of China.
Xinjian LinKey Laboratory of Gastrointestinal Cancer (Fujian Medical University), Ministry of Education , Fuzhou , People's Republic of China.
Xu LinKey Laboratory of Gastrointestinal Cancer (Fujian Medical University), Ministry of Education , Fuzhou , People's Republic of China.
Fujian Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HBx is a short-lived protein whose rapid turnover is mainly regulated by ubiquitin-dependent proteasomal degradation pathways. Our prior work identified BAF155 to be one of the HBx binding partners. Since BAF155 has been shown to stabilize other members of the SWI/SNF chromatin remodelling complex by attenuating their proteasomal degradation, we proposed that BAF155 might also contribute to stabilizing HBx protein in a proteasome-dependent manner. Here we report that BAF155 protected hepatitis B virus X protein (HBx) from ubiquitin-independent proteasomal degradation by competing with the 20S proteasome subunit PSMA7 to bind to HBx. BAF155 was found to directly interact with HBx via binding of its SANT domain to the HBx region between amino acid residues 81 and 120. Expression of either full-length BAF155 or SANT domain increased HBx protein levels whereas siRNA-mediated knockdown of endogenous BAF155 reduced HBx protein levels. Increased HBx stability and steady-state level by BAF155 were attributable to inhibition of ubiquitin-independent and PSMA7-mediated protein degradation. Consequently, overexpression of BAF155 enhanced the transcriptional transactivation function of HBx, activated protooncogene expression and inhibited hepatoma cell clonogenicity. These results suggest that BAF155 plays important roles in ubiquitin-independent degradation of HBx, which may be related to the pathogenesis and carcinogenesis of HBV-associated HCC.

Indexed as

Carcinoma, HepatocellularCell LineChromatin Assembly and DisassemblyHepatitis BHepatitis B virusHep G2 CellsHumansLiver NeoplasmsProteasome Endopeptidase ComplexTrans-ActivatorsTranscription FactorsUbiquitinViral Regulatory and Accessory ProteinsVirus Replicationhepatitis B virus X proteinProteasome Endopeptidase ComplexPSMA7 protein, humanSMARCC1 protein, humanTrans-ActivatorsTranscription FactorsUbiquitinViral Regulatory and Accessory Proteinschromatin remodelling factor BAF155Hepatitis B virus X proteinhpatocellular carcinomaproteasomal subunit PSMA7ubiquitin-dependent and -independent proteasomal degradation

Identifiers

PMID31533543
PMCPMC6758689
OpenAlexW2974046205

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.