Evidence map›Paper›PMID 32203489›Full record

ArticleNature structural & molecular biology2020

Roles of the BRD4 short isoform in phase separation and active gene transcription.

Xinye Han, Di Yu, Ruirui Gu, Yanjie Jia, Qi Wang, Anbalagan Jaganathan, Xuelan Yang, Miaomiao Yu, Nicolas Babault, Chengcheng Zhao and 4 more

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed
7.0field-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

106 citing papers in PubMed, 166 citations in OpenAlex.

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46 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

14 authors at 3 institutions in 2 countries.

Xinye Han *Bethune Institute of Epigenetic Medicine, The First Hospital, Jilin University, Changchun, Jilin, China.
Di Yu *Bethune Institute of Epigenetic Medicine, The First Hospital, Jilin University, Changchun, Jilin, China.ORCID http://orcid.org/0000-0001-9947-0624
Ruirui GuBethune Institute of Epigenetic Medicine, The First Hospital, Jilin University, Changchun, Jilin, China.
Yanjie JiaBethune Institute of Epigenetic Medicine, The First Hospital, Jilin University, Changchun, Jilin, China.
Qi WangBethune Institute of Epigenetic Medicine, The First Hospital, Jilin University, Changchun, Jilin, China.
Anbalagan JaganathanDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA.
Xuelan YangBethune Institute of Epigenetic Medicine, The First Hospital, Jilin University, Changchun, Jilin, China.
Miaomiao YuBethune Institute of Epigenetic Medicine, The First Hospital, Jilin University, Changchun, Jilin, China.
Nicolas BabaultDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA.
Chengcheng ZhaoBethune Institute of Epigenetic Medicine, The First Hospital, Jilin University, Changchun, Jilin, China.
Huanfa YiBethune Institute of Epigenetic Medicine, The First Hospital, Jilin University, Changchun, Jilin, China.
Qiang ZhangBethune Institute of Epigenetic Medicine, The First Hospital, Jilin University, Changchun, Jilin, China.
Ming-Ming ZhouDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA. ming-ming.zhou@mssm.edu.ORCID http://orcid.org/0000-0002-7049-0573
Lei ZengBethune Institute of Epigenetic Medicine, The First Hospital, Jilin University, Changchun, Jilin, China. leizeng@jlu.edu.cn.ORCID http://orcid.org/0000-0002-4236-6735
Jilin University · CNFirst Bethune Hospital of Jilin University · CNIcahn School of Medicine at Mount Sinai · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

BRD4, a major tandem-bromodomain-containing transcription regulator, has two isoforms. The long isoform (BRD4L) has an extended C terminus that binds transcription cofactors, while the short isoform (BRD4S) lacks this C-terminal extension. Unlike BRD4L, the role of BRD4S in gene transcription remains unclear. Here, we report that, in human cancer cells, BRD4S forms nuclear puncta that possess liquid-like properties and that colocalize with BRD4L, MED1 and sites of histone H3 lysine 27 acetylation. BRD4 puncta are correlated with BRD4S but not BRD4L expression levels. BRD4S knockdown reduces BRD4S condensation, and ectopic expression promotes puncta formation and target gene transcription. BRD4S nuclear condensation is mediated by its intrinsically disordered regions and binding of its bromodomains to DNA and acetylated chromatin, respectively, and BRD4S phosphorylation diminishes BRD4 condensation. Our study illuminates a previously unappreciated role of BRD4S in organizing chromatin and transcription factors through phase separation to sustain gene transcription in chromatin for cancer cell proliferation.

Indexed as

A549 CellsAcetylationBromodomain Containing ProteinsCell Cycle ProteinsCell ProliferationChromatinDNA-Binding ProteinsGene Expression Regulation, NeoplasticHistonesHumansMediator Complex Subunit 1NeoplasmsProtein IsoformsTranscription FactorsBRD4 protein, humanBromodomain Containing ProteinsCell Cycle ProteinsChromatinDNA-Binding ProteinsHistonesMED1 protein, humanMediator Complex Subunit 1Protein IsoformsTranscription Factors

Identifiers

PMID32203489
OpenAlexW3010650772

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.