Evidence map›Paper›PMID 26848759›Full record

ArticlePloS one2016

The Arginine Methyltransferase PRMT6 Cooperates with Polycomb Proteins in Regulating HOXA Gene Expression.

Claudia Stein, René Reiner Nötzold, Stefanie Riedl, Caroline Bouchard, Uta-Maria Bauer

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. The Emerging Role of PRMT6 in Cancer.Frontiers in oncology · 2022
    Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Roles and regulation of histone methylation in animal development.Nature reviews. Molecular cell biology · 2019
    Review
  14. Article
  15. Review
  16. Article
  17. 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

5 authors at 1 institution in 1 country.

Claudia SteinInstitute for Molecular Biology and Tumor Research (IMT), Philipps-University of Marburg, Marburg, Germany.
René Reiner NötzoldInstitute for Molecular Biology and Tumor Research (IMT), Philipps-University of Marburg, Marburg, Germany.
Stefanie RiedlInstitute for Molecular Biology and Tumor Research (IMT), Philipps-University of Marburg, Marburg, Germany.
Caroline BouchardInstitute for Molecular Biology and Tumor Research (IMT), Philipps-University of Marburg, Marburg, Germany.
Uta-Maria BauerInstitute for Molecular Biology and Tumor Research (IMT), Philipps-University of Marburg, Marburg, Germany.
Philipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein arginine methyltransferase 6 (PRMT6) catalyses asymmetric dimethylation of histone H3 at arginine 2 (H3R2me2a), which has been shown to impede the deposition of histone H3 lysine 4 trimethylation (H3K4me3) by blocking the binding and activity of the MLL1 complex. Importantly, the genomic occurrence of H3R2me2a has been found to coincide with histone H3 lysine 27 trimethylation (H3K27me3), a repressive histone mark generated by the Polycomb repressive complex 2 (PRC2). Therefore, we investigate here a putative crosstalk between PRMT6- and PRC-mediated repression in a cellular model of neuronal differentiation. We show that PRMT6 and subunits of PRC2 as well as PRC1 are bound to the same regulatory regions of rostral HOXA genes and that they control the differentiation-associated activation of these genes. Furthermore, we find that PRMT6 interacts with subunits of PRC1 and PRC2 and that depletion of PRMT6 results in diminished PRC1/PRC2 and H3K27me3 occupancy and in increased H3K4me3 levels at these target genes. Taken together, our data uncover a novel, additional mechanism of how PRMT6 contributes to gene repression by cooperating with Polycomb proteins.

Indexed as

Gene Expression RegulationCell DifferentiationCell LineHEK293 CellsHistonesHomeodomain ProteinsHumansNeuronsNuclear ProteinsPolycomb-Group ProteinsProtein-Arginine N-MethyltransferasesHistonesHomeodomain ProteinsHoxA proteinNuclear ProteinsPolycomb-Group ProteinsPRMT6 protein, humanProtein-Arginine N-Methyltransferases

Identifiers

PMID26848759
PMCPMC4746130
OpenAlexW2260267530

What OpenQuestion holds

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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.