Evidence map›Paper›PMID 32446320›Full record

ArticleMolecular cell2020

Opposing Functions of BRD4 Isoforms in Breast Cancer.

Shwu-Yuan Wu, Chien-Fei Lee, Hsien-Tsung Lai, Cheng-Tai Yu, Ji-Eun Lee, Hao Zuo, Sophia Y Tsai, Ming-Jer Tsai, Kai Ge, Yihong Wan and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
10.4field-weighted citation impact, top 1% 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

94 citing papers in PubMed, 206 citations in OpenAlex.

  1. SRSF3 plays a key role in liver cancer sex disparity by facilitating hepatocyte expression of ERα and FOXA.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  7. Development of PolyHis-Targeting PROTAC Degraders.Angewandte Chemie (International ed. in English) · 2026
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34 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 1 country.

Shwu-Yuan WuSimmons Comprehensive Cancer Center, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Chien-Fei LeeSimmons Comprehensive Cancer Center, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Hsien-Tsung LaiSimmons Comprehensive Cancer Center, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Cheng-Tai YuDepartment of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Ji-Eun LeeAdipocyte Biology and Gene Regulation Section, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Hao ZuoDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Sophia Y TsaiDepartment of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Ming-Jer TsaiDepartment of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Kai GeAdipocyte Biology and Gene Regulation Section, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Yihong WanSimmons Comprehensive Cancer Center, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Cheng-Ming ChiangSimmons Comprehensive Cancer Center, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Electronic address: cheng-ming.chiang@utsouthwestern.edu.
The University of Texas Southwestern Medical Center · USBaylor College of Medicine · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Regulation of PPARgamma Expression and Adipogenesis by PTIP-Associated FactorsZIADK075003 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI GE, KAI · 2009 to 2025
$17.6M
Epigenomic Regulation of PPARgamma and AdipogenesisZIADK075017 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI GE, KAI · 2009 to 2025
$12.4M
Opposing Functions of BRD4 Isoforms in Breast CancerR01CA251698 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI CHIANG, CHENG-MING · 2020 to 2024
$2.3M
Context-Dependent Effects of PARP Inhibitors on Breast Cancer Bone MetastasisR01CA229487 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI KRAUS, WILLIAM LEE · 2018 to 2023
$1.8M
Novel Mechanisms of Cancer Bone MetastasisR01CA236802 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI WAN, YIHONG · 2019 to 2020
$741k
Department of Defense W81XWH-18-1-0014NCI NIH HHS R01 CA229487NCI NIH HHS R01 CA236802NCI NIH HHS R01 CA251698
6 · The paper itself

Abstract

Bromodomain-containing protein 4 (BRD4) is a cancer therapeutic target in ongoing clinical trials disrupting primarily BRD4-regulated transcription programs. The role of BRD4 in cancer has been attributed mainly to the abundant long isoform (BRD4-L). Here we show, by isoform-specific knockdown and endogenous protein detection, along with transgene expression, the less abundant BRD4 short isoform (BRD4-S) is oncogenic while BRD4-L is tumor-suppressive in breast cancer cell proliferation and migration, as well as mammary tumor formation and metastasis. Through integrated RNA-seq, genome-wide ChIP-seq, and CUT&RUN association profiling, we identify the Engrailed-1 (EN1) homeobox transcription factor as a key BRD4-S coregulator, particularly in triple-negative breast cancer. BRD4-S and EN1 comodulate the extracellular matrix (ECM)-associated matrisome network, including type II cystatin gene cluster, mucin 5, and cathepsin loci, via enhancer regulation of cancer-associated genes and pathways. Our work highlights the importance of targeted therapies for the oncogenic, but not tumor-suppressive, activity of BRD4.

Indexed as

AnimalsBreast NeoplasmsBromodomain Containing ProteinsCell Cycle ProteinsCell Line, TumorCell MovementCell ProliferationFemaleGene Expression Regulation, NeoplasticGenes, HomeoboxHomeodomain ProteinsHumansMiceNeoplasm InvasivenessNuclear ProteinsProtein IsoformsBRD4 protein, humanbromodomain and extra-terminal domain protein, humanBromodomain Containing ProteinsCell Cycle ProteinsEN1 protein, humanHomeodomain ProteinsNuclear ProteinsProtein IsoformsProteinsTranscription FactorsBET inhibitorBRD4bromodomainCUT&RUNdrug resistanceECMenhancerepigeneticsTNBCtranscription factor

Identifiers

PMID32446320
PMCPMC7362310
OpenAlexW3027413721

What OpenQuestion holds

Textmetadata
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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.