Evidence map›Paper›PMID 30327463›Full record

ArticleNature communications2018

PWWP2A binds distinct chromatin moieties and interacts with an MTA1-specific core NuRD complex.

Stephanie Link, Ramona M M Spitzer, Maryam Sana, Mario Torrado, Moritz C Völker-Albert, Eva C Keilhauer, Thomas Burgold, Sebastian Pünzeler, Jason K K Low, Ida Lindström and 9 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

34 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Two High-QualityInternational journal of molecular sciences · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. RNA mMolecular therapy : the journal of the American Society of Gene Therapy · 2022
    Article
  18. Article
  19. Article
  20. PWWP2B Fine-Tunes Adipose Thermogenesis by Stabilizing HDACs in a NuRD Subcomplex.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021
    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

19 authors at 8 institutions in 4 countries.

Stephanie LinkDepartment of Molecular Biology, BioMedical Center (BMC), Ludwig-Maximilians-University Munich, 82152, Planegg-Martinsried, Germany.
Ramona M M SpitzerDepartment of Molecular Biology, BioMedical Center (BMC), Ludwig-Maximilians-University Munich, 82152, Planegg-Martinsried, Germany.
Maryam SanaSchool of Life and Environmental Sciences, University of Sydney, New South Wales, 2006, Australia.
Mario TorradoSchool of Life and Environmental Sciences, University of Sydney, New South Wales, 2006, Australia.
Moritz C Völker-AlbertDepartment of Molecular Biology, BioMedical Center (BMC), Ludwig-Maximilians-University Munich, 82152, Planegg-Martinsried, Germany.
Eva C KeilhauerDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152, Martinsried, Germany.
Thomas BurgoldWellcome Trust - MRC Stem Cell Institute and Department of Biochemistry, University of Cambridge, Cambridge, CB2 1QR, UK.
Sebastian PünzelerDepartment of Molecular Biology, BioMedical Center (BMC), Ludwig-Maximilians-University Munich, 82152, Planegg-Martinsried, Germany.
Jason K K LowSchool of Life and Environmental Sciences, University of Sydney, New South Wales, 2006, Australia.
Ida LindströmSchool of Life and Environmental Sciences, University of Sydney, New South Wales, 2006, Australia.ORCID http://orcid.org/0000-0002-0405-778X
Andrea NistGenomics Core Facility, Philipps-University Marburg, 35043, Marburg, Germany.
Catherine RegnardDepartment of Molecular Biology, BioMedical Center (BMC), Ludwig-Maximilians-University Munich, 82152, Planegg-Martinsried, Germany.
Thorsten StieweGenomics Core Facility, Philipps-University Marburg, 35043, Marburg, Germany.ORCID http://orcid.org/0000-0003-0134-7826
Brian HendrichWellcome Trust - MRC Stem Cell Institute and Department of Biochemistry, University of Cambridge, Cambridge, CB2 1QR, UK.
Axel ImhofDepartment of Molecular Biology, BioMedical Center (BMC), Ludwig-Maximilians-University Munich, 82152, Planegg-Martinsried, Germany.ORCID http://orcid.org/0000-0003-2993-8249
Matthias MannDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152, Martinsried, Germany.ORCID http://orcid.org/0000-0003-1292-4799
Joel P MackaySchool of Life and Environmental Sciences, University of Sydney, New South Wales, 2006, Australia.ORCID http://orcid.org/0000-0001-7508-8033
Marek BartkuhnInstitute for Genetics, Justus-Liebig University Giessen, 35392, Giessen, Germany. marek.bartkuhn@gen.bio.uni-giessen.
Sandra B HakeInstitute for Genetics, Justus-Liebig University Giessen, 35392, Giessen, Germany. sandra.hake@gen.bio.uni-giessen.de.ORCID http://orcid.org/0000-0003-0029-6588
The University of Sydney · AUCenter for Integrated Protein Science Munich · DEJustus-Liebig-Universität Gießen · DELudwig-Maximilians-Universität München · DEPhilipps University of Marburg · DEWellcome/MRC Cambridge Stem Cell Institute · GBAtlas Copco (Germany) · DEMax Planck Institute of Biochemistry · DE

Funding

Medical Research Council MC_PC_12009Wellcome Trust
6 · The paper itself

Abstract

Chromatin structure and function is regulated by reader proteins recognizing histone modifications and/or histone variants. We recently identified that PWWP2A tightly binds to H2A.Z-containing nucleosomes and is involved in mitotic progression and cranial-facial development. Here, using in vitro assays, we show that distinct domains of PWWP2A mediate binding to free linker DNA as well as H3K36me3 nucleosomes. In vivo, PWWP2A strongly recognizes H2A.Z-containing regulatory regions and weakly binds H3K36me3-containing gene bodies. Further, PWWP2A binds to an MTA1-specific subcomplex of the NuRD complex (M1HR), which consists solely of MTA1, HDAC1, and RBBP4/7, and excludes CHD, GATAD2 and MBD proteins. Depletion of PWWP2A leads to an increase of acetylation levels on H3K27 as well as H2A.Z, presumably by impaired chromatin recruitment of M1HR. Thus, this study identifies PWWP2A as a complex chromatin-binding protein that serves to direct the deacetylase complex M1HR to H2A.Z-containing chromatin, thereby promoting changes in histone acetylation levels.

Indexed as

AcetylationAnimalsChromatinChromosomal Proteins, Non-HistoneHEK293 CellsHistone DeacetylasesHistonesHumansLysineMethylationMi-2 Nucleosome Remodeling and Deacetylase ComplexMiceNucleosomesRepressor ProteinsRNA, Small InterferingTrans-ActivatorsChromatinChromosomal Proteins, Non-HistoneHistone Deacetylaseshistone H2A.F-ZHistonesLysineMi-2 Nucleosome Remodeling and Deacetylase ComplexMTA1 protein, humanNucleosomesPWWP2A protein, humanRepressor ProteinsRNA, Small InterferingTrans-Activators

Identifiers

PMID30327463
PMCPMC6191444
OpenAlexW2896482046

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.