Evidence map›Paper›PMID 20671031›Full record

ArticleNucleic acids research2010

The phosphatase interactor NIPP1 regulates the occupancy of the histone methyltransferase EZH2 at Polycomb targets.

Nele Van Dessel, Lijs Beke, Janina Görnemann, Nikki Minnebo, Monique Beullens, Nobuhiro Tanuma, Hiroshi Shima, Aleyde Van Eynde, Mathieu Bollen

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Sut-6/NIPP1 modulates tau toxicity.Human molecular genetics · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Protein phosphatases in chromatin structure and function.Biochimica et biophysica acta. Molecular cell research · 2019
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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  19. Review
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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

9 authors at 2 institutions in 2 countries.

Nele Van DesselLaboratory of Biosignaling and Therapeutics, Department of Molecular Cell Biology, Faculty of Medicine, KULeuven, B-3000 Leuven, Belgium.
Lijs Beke
Janina Görnemann
Nikki Minnebo
Monique Beullens
Nobuhiro Tanuma
Hiroshi Shima
Aleyde Van Eynde
Mathieu Bollen
KU Leuven · BEMiyagi Prefectural Hospital Organization · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polycomb group (PcG) proteins are key regulators of stem-cell and cancer biology. They mainly act as repressors of differentiation and tumor-suppressor genes. One key silencing step involves the trimethylation of histone H3 on Lys27 (H3K27) by EZH2, a core component of the Polycomb Repressive Complex 2 (PRC2). The mechanism underlying the initial recruitment of mammalian PRC2 complexes is not well understood. Here, we show that NIPP1, a regulator of protein Ser/Thr phosphatase-1 (PP1), forms a complex with PP1 and PRC2 components on chromatin. The knockdown of NIPP1 or PP1 reduced the association of EZH2 with a subset of its target genes, whereas the overexpression of NIPP1 resulted in a retargeting of EZH2 from fully repressed to partially active PcG targets. However, the expression of a PP1-binding mutant of NIPP1 (NIPP1m) did not cause a redistribution of EZH2. Moreover, mapping of the chromatin binding sites with the DamID technique revealed that NIPP1 was associated with multiple PcG target genes, including the Homeobox A cluster, whereas NIPP1m showed a deficient binding at these loci. We propose that NIPP1 associates with a subset of PcG targets in a PP1-dependent manner and thereby contributes to the recruitment of the PRC2 complex.

Indexed as

Binding SitesCell LineChromatinDNA-Binding ProteinsEndoribonucleasesEnhancer of Zeste Homolog 2 ProteinHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHumansPhosphoprotein PhosphatasesPolycomb-Group ProteinsPolycomb Repressive Complex 2Promoter Regions, GeneticProtein Phosphatase 1Repressor ProteinsRNA-Binding ProteinsChromatinDNA-Binding ProteinsEndoribonucleasesEnhancer of Zeste Homolog 2 ProteinEZH2 protein, humanHistone-Lysine N-MethyltransferaseHistone MethyltransferasesPhosphoprotein PhosphatasesPolycomb-Group ProteinsPolycomb Repressive Complex 2PPP1R8 protein, humanProtein Phosphatase 1Repressor ProteinsRNA-Binding ProteinsTranscription Factors

Identifiers

PMID20671031
PMCPMC2995064
OpenAlexW2067658363

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.