Evidence map›Paper›PMID 41478281›Full record

ArticleMolecular cell2026

BRD2 bridges TFIID and MOF-H4K16ac-containing nucleosomes to promote transcriptional initiation.

Bin Zheng, Ruxuan Qiu, Sarah Gold, Marta Iwanaszko, Yuki Aoi, Benjamin Charles Howard, Madhurima Das, Ali Shilatifard

Abstract read
In one paragraph

Article in Molecular cell, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. The molecular basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2026
    Review
  3. Article
  4. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Bin ZhengSimpson Querrey Institute for Epigenetics and the Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA. Electronic address: bin.zheng@northwestern.edu.
Ruxuan QiuSimpson Querrey Institute for Epigenetics and the Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Sarah GoldSimpson Querrey Institute for Epigenetics and the Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Marta IwanaszkoSimpson Querrey Institute for Epigenetics and the Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Yuki AoiSimpson Querrey Institute for Epigenetics and the Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Benjamin Charles HowardSimpson Querrey Institute for Epigenetics and the Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Madhurima DasSimpson Querrey Institute for Epigenetics and the Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Ali ShilatifardSimpson Querrey Institute for Epigenetics and the Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA; Chan Zuckerberg Biohub Chicago, Chicago, IL 60642, USA. Electronic address: ash@northwestern.edu.

Funding

Mutations of Chromatin and its Modifying Machineries in MalignanciesR35CA197569 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Ali Shilatifard · 2015 to 2026
$10.7M
Computational Approaches for Studying Transcription Elongation Control in CancerR50CA265372 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Marta Iwanaszko · 2022 to 2026
$722k
NCI NIH HHS R35 CA197569NCI NIH HHS R50 CA265372
6 · The paper itself

Abstract

Members of the bromodomain and extraterminal domain (BET) protein family play a central role in transcription by RNA polymerase II (RNA Pol II). Small-molecule inhibitors that block interaction between BET bromodomains and acetylated histones have been developed for disease therapeutics. However, the BET protein BRD4 does not require bromodomains to perform its major transcriptional elongation control, and mechanisms by which other BET proteins regulate RNA Pol II remain insufficiently understood. Addressing the disparity between pan-BET degraders and BRD4-specific depletion, we report that the BET protein BRD2 generally functions to promote transcriptional initiation in a bromodomain-dependent manner at both promoters and enhancers in human cell lines. We demonstrate that BRD2 bromodomains preferentially bind to histone H4 harboring MOF-mediated H4K16ac, while the BRD2 C-terminal domain facilitates recruitment of TFIID. Our studies provide mechanistic insight into distinct roles for BRD2 and BRD4 in transcriptional initiation and elongation control for proper regulation of gene expression.

Indexed as

Histone AcetyltransferasesHistonesNucleosomesProtein Serine-Threonine KinasesTranscription FactorsTranscription Factor TFIIDTranscription Initiation, GeneticAcetylationBromodomain Containing ProteinsCell Cycle ProteinsEnhancer Elements, GeneticGene Expression RegulationHEK293 CellsHumansNuclear ProteinsPromoter Regions, GeneticBRD2 protein, humanBRD4 protein, humanBromodomain Containing ProteinsCell Cycle ProteinsHistone AcetyltransferasesHistonesNuclear ProteinsNucleosomesProtein Serine-Threonine KinasesRNA Polymerase IITranscription FactorsTranscription Factor TFIIDBET inhibitorsBRD2BRD4chromatindBET6gene expressionH4K16acJQ1MOFRNA polymerase IITFIIDtranscriptiontranscription initiation

Identifiers

PMID41478281
PMCPMC13576088

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.