Evidence map›Paper›PMID 28533407›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Histone-binding of DPF2 mediates its repressive role in myeloid differentiation.

Ferdinand M Huber, Sarah M Greenblatt, Andrew M Davenport, Concepcion Martinez, Ye Xu, Ly P Vu, Stephen D Nimer, André Hoelz

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

28 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. TheInternational journal of molecular sciences · 2024
    Article
  7. DPF2 reads histone lactylation to drive transcription and tumorigenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  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

8 authors at 4 institutions in 1 country.

Ferdinand M HuberDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125.
Sarah M GreenblattSylvester Comprehensive Cancer Center, University of Miami Miller School of Medicine, Miami, FL 33136.
Andrew M DavenportDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125.
Concepcion MartinezSylvester Comprehensive Cancer Center, University of Miami Miller School of Medicine, Miami, FL 33136.
Ye XuSylvester Comprehensive Cancer Center, University of Miami Miller School of Medicine, Miami, FL 33136.
Ly P VuMolecular Pharmacology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065.
Stephen D NimerSylvester Comprehensive Cancer Center, University of Miami Miller School of Medicine, Miami, FL 33136; snimer@med.miami.edu hoelz@caltech.edu.
André HoelzDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125; snimer@med.miami.edu hoelz@caltech.edu.
California Institute of Technology · USSylvester Comprehensive Cancer Center · USMemorial Sloan Kettering Cancer Center · USUniversity of Miami · US

Funding

PREDOCTORAL TRAINING IN BIOLOGY AND CHEMISTRYT32GM007616 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI STERNBERG, PAUL WARREN · 1985 to 2019
$22.9M
Targeting p300 and lysine acetylation in AMLR01CA166835 · NCI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI Stephen D. Nimer · 2012 to 2026
$4.6M
Molecular Basis of mRNA ExportR01GM117360 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI Andre Hoelz · 2016 to 2026
$2.6M
Howard Hughes Medical InstituteNCI NIH HHS R01 CA166835NIGMS NIH HHS R01 GM117360NIGMS NIH HHS T32 GM007616
6 · The paper itself

Abstract

Double plant homeodomain finger 2 (DPF2) is a highly evolutionarily conserved member of the d4 protein family that is ubiquitously expressed in human tissues and was recently shown to inhibit the myeloid differentiation of hematopoietic stem/progenitor and acute myelogenous leukemia cells. Here, we present the crystal structure of the tandem plant homeodomain finger domain of human DPF2 at 1.6-Å resolution. We show that DPF2 interacts with the acetylated tails of both histones 3 and 4 via bipartite binding pockets on the DPF2 surface. Blocking these interactions through targeted mutagenesis of DPF2 abolishes its recruitment to target chromatin regions as well as its ability to prevent myeloid differentiation in vivo. Our findings suggest that the histone binding of DPF2 plays an important regulatory role in the transcriptional program that drives myeloid differentiation.

Indexed as

AcetylationCell DifferentiationChromatinCrystallography, X-RayDNA-Binding ProteinsHematopoiesisHistonesHumansModels, MolecularMyeloid CellsProtein BindingProtein DomainsTranscription FactorsChromatinDNA-Binding ProteinsDPF2 protein, humanHistonesTranscription Factorsisothermal titration calorimetrymyeloid differentiationprotein–protein interactiontandem PHD fingerX-ray crystallography

Identifiers

PMID28533407
PMCPMC5468650
OpenAlexW2617976371

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.