Evidence map›Paper›PMID 29567837›Full record

ArticleThe Journal of biological chemistry2018

The BRD3 ET domain recognizes a short peptide motif through a mechanism that is conserved across chromatin remodelers and transcriptional regulators.

Dorothy C C Wai, Taylor N Szyszka, Amy E Campbell, Cherry Kwong, Lorna E Wilkinson-White, Ana P G Silva, Jason K K Low, Ann H Kwan, Roland Gamsjaeger, James D Chalmers and 5 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

41 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Loop Plasticity Drives Paralog-Specific Recognition in BET ET Domains.Journal of chemical information and modeling · 2026
    Article
  3. Article
  4. Article
  5. Chromodomain helicase DNA-binding proteins and orofacial cleft.Journal of research in medical sciences : the official journal of Isfahan University of Medical Sciences · 2026
    Review
  6. Article
  7. Loop Plasticity Drives Paralog-Specific Recognition in BET ET Domains.bioRxiv : the preprint server for biology · 2025
    Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. How does CHD4 slide nucleosomes?Biochemical Society transactions · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article
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

15 authors at 4 institutions in 3 countries.

Dorothy C C WaiSchool of Life and Environmental Sciences, University of Sydney New South Wales 2006, Australia.
Taylor N SzyszkaSchool of Life and Environmental Sciences, University of Sydney New South Wales 2006, Australia.
Amy E CampbellDivision of Hematology, Children's Hospital of Philadelphia, and the Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104.
Cherry KwongSchool of Life and Environmental Sciences, University of Sydney New South Wales 2006, Australia.
Lorna E Wilkinson-WhiteSchool of Life and Environmental Sciences, University of Sydney New South Wales 2006, Australia.
Ana P G SilvaSchool of Life and Environmental Sciences, University of Sydney New South Wales 2006, Australia.
Jason K K LowSchool of Life and Environmental Sciences, University of Sydney New South Wales 2006, Australia.
Ann H KwanSchool of Life and Environmental Sciences, University of Sydney New South Wales 2006, Australia.
Roland GamsjaegerSchool of Life and Environmental Sciences, University of Sydney New South Wales 2006, Australia.
James D ChalmersDepartment of Biochemistry, University of Otago, Dunedin 9016, New Zealand.
Wayne M PatrickDepartment of Biochemistry, University of Otago, Dunedin 9016, New Zealand.
Bin LuCold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724.
Christopher R VakocCold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724.
Gerd A BlobelDivision of Hematology, Children's Hospital of Philadelphia, and the Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104.
Joel P MackaySchool of Life and Environmental Sciences, University of Sydney New South Wales 2006, Australia. Electronic address: joel.mackay@sydney.edu.au.
University of Sydney · AUChildren's Hospital of Philadelphia · USCold Spring Harbor Laboratory · USUniversity of Otago · NZ

Funding

Transcriptional Networks Controlling Erythroid DifferentiationR01DK054937 · NIDDK · CHILDREN'S HOSP OF PHILADELPHIA · PI Gerd A Blobel · 1999 to 2026
$12.8M
HEMATOPOIESIS TRAINING GRANTT32DK007780 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI TONG, WEI · 1999 to 2023
$6.7M
BET bromodomain inhibition as targeted therapy in acute myeloid leukemiaR01CA174793 · NCI · COLD SPRING HARBOR LABORATORY · PI VAKOC, CHRISTOPHER · 2013 to 2023
$5.5M
NCI NIH HHS R01 CA174793NIDDK NIH HHS R01 DK054937NIDDK NIH HHS T32 DK007780
6 · The paper itself

Abstract

Members of the bromodomain and extra-terminal domain (BET) family of proteins (bromodomain-containing (BRD) 2, 3, 4, and T) are widely expressed and highly conserved regulators of gene expression in eukaryotes. These proteins have been intimately linked to human disease, and more than a dozen clinical trials are currently underway to test BET-protein inhibitors as modulators of cancer. However, although it is clear that these proteins use their bromodomains to bind both histones and transcription factors bearing acetylated lysine residues, the molecular mechanisms by which BET family proteins regulate gene expression are not well defined. In particular, the functions of the other domains such as the ET domain have been less extensively studied. Here, we examine the properties of the ET domain of BRD3 as a protein/protein interaction module. Using a combination of pulldown and biophysical assays, we demonstrate that BRD3 binds to a range of chromatin-remodeling complexes, including the NuRD, BAF, and INO80 complexes, via a short linear "KIKL" motif in one of the complex subunits. NMR-based structural analysis revealed that, surprisingly, this mode of interaction is shared by the AF9 and ENL transcriptional coregulators that contain an acetyl-lysine-binding YEATS domain and regulate transcriptional elongation. This observation establishes a functional commonality between these two families of cancer-related transcriptional regulators. In summary, our data provide insight into the mechanisms by which BET family proteins might link chromatin acetylation to transcriptional outcomes and uncover an unexpected functional similarity between BET and YEATS family proteins.

Indexed as

Chromatin Assembly and DisassemblyAcetylationAmino Acid MotifsAmino Acid SequenceATPases Associated with Diverse Cellular ActivitiesBiophysical PhenomenaBromodomain Containing ProteinsDNA-Binding ProteinsDNA HelicasesGene Expression RegulationGene Regulatory NetworksHEK293 CellsHumansMi-2 Nucleosome Remodeling and Deacetylase ComplexNuclear ProteinsPeptidesATPases Associated with Diverse Cellular ActivitiesBANF1 protein, humanBRD3 protein, humanBromodomain Containing ProteinsCHD4 protein, humanDNA-Binding ProteinsDNA HelicasesINO80 protein, humanMi-2 Nucleosome Remodeling and Deacetylase ComplexNuclear ProteinsPeptidesRNA-Binding ProteinsTrans-ActivatorsTranscription FactorsacetylationAF9BET family proteinsbromodomainextraterminal domainnuclear magnetic resonance (NMR)protein/protein interactionprotein structuretranscriptional coactivator

Identifiers

PMID29567837
PMCPMC5949996
OpenAlexW2790990664

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.