Evidence map›Paper›PMID 30228260›Full record

ArticleNature communications2018

A variant NuRD complex containing PWWP2A/B excludes MBD2/3 to regulate transcription at active genes.

Tianyi Zhang, Guifeng Wei, Christopher J Millard, Roman Fischer, Rebecca Konietzny, Benedikt M Kessler, John W R Schwabe, Neil Brockdorff

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 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 54 citations in OpenAlex.

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  20. PWWP2B Fine-Tunes Adipose Thermogenesis by Stabilizing HDACs in a NuRD Subcomplex.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021
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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 2 institutions in 2 countries.

Tianyi ZhangDevelopmental Epigenetics, Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, United Kingdom.
Guifeng WeiDevelopmental Epigenetics, Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, United Kingdom.ORCID http://orcid.org/0000-0002-5698-426X
Christopher J MillardLeicester Institute for Structural and Chemical Biology and Department of Molecular and Cell Biology, University of Leicester, Leicester, LE1 7RH, United Kingdom.ORCID http://orcid.org/0000-0002-1012-0829
Roman FischerTarget Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ, United Kingdom.ORCID http://orcid.org/0000-0002-9715-5951
Rebecca KonietznyTarget Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ, United Kingdom.
Benedikt M KesslerTarget Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ, United Kingdom.ORCID http://orcid.org/0000-0002-8160-2446
John W R SchwabeLeicester Institute for Structural and Chemical Biology and Department of Molecular and Cell Biology, University of Leicester, Leicester, LE1 7RH, United Kingdom.ORCID http://orcid.org/0000-0003-2865-4383
Neil BrockdorffDevelopmental Epigenetics, Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, United Kingdom. neil.brockdorff@bioch.ox.ac.uk.
University of Oxford · GBUniversity of Leicester · GB

Funding

European Research Council 340081Wellcome Trust 100237/Z/12/ZWellcome Trust 103768
6 · The paper itself

Abstract

Transcriptional regulation by chromatin is a highly dynamic process directed through the recruitment and coordinated action of epigenetic modifiers and readers of these modifications. Using an unbiased proteomic approach to find interactors of H3K36me3, a modification enriched on active chromatin, here we identify PWWP2A and HDAC2 among the top interactors. PWWP2A and its paralog PWWP2B form a stable complex with NuRD subunits MTA1/2/3:HDAC1/2:RBBP4/7, but not with MBD2/3, p66α/β, and CHD3/4. PWWP2A competes with MBD3 for binding to MTA1, thus defining a new variant NuRD complex that is mutually exclusive with the MBD2/3 containing NuRD. In mESCs, PWWP2A/B is most enriched at highly transcribed genes. Loss of PWWP2A/B leads to increases in histone acetylation predominantly at highly expressed genes, accompanied by decreases in Pol II elongation. Collectively, these findings suggest a role for PWWP2A/B in regulating transcription through the fine-tuning of histone acetylation dynamics at actively transcribed genes.

Indexed as

Gene Expression RegulationTranscription Elongation, GeneticAcetylationAnimalsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDNA MethylationGene Knockout TechniquesHEK293 CellsHeLa CellsHumansMi-2 Nucleosome Remodeling and Deacetylase ComplexMiceMouse Embryonic Stem CellsNucleosomesProteomicsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsMBD2 protein, humanMBD3 protein, humanMi-2 Nucleosome Remodeling and Deacetylase ComplexNucleosomesPWWP2A protein, humanPwwp2a protein, mousePWWP2B protein, humanPwwp2b protein, mouseRNA Polymerase II

Identifiers

PMID30228260
PMCPMC6143588
OpenAlexW2890288614

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.