Evidence map›Paper›PMID 16415179›Full record

ArticleNucleic acids research2006

p66alpha and p66beta of the Mi-2/NuRD complex mediate MBD2 and histone interaction.

Marc Brackertz, Zihua Gong, Jörg Leers, Rainer Renkawitz

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

49 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
  6. It Takes a Village of Chromatin Remodelers to Regulate rDNA Expression.International journal of molecular sciences · 2025
    Review
  7. Article
  8. Article
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  10. Article
  11. HGG advances · 2023
    Article
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  19. GATAD2B-associated neurodevelopmental disorder (GAND): clinical and molecular insights into a NuRD-related disorder.Genetics in medicine : official journal of the American College of Medical Genetics · 2020
    Article
  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

4 authors at 1 institution in 1 country.

Marc BrackertzInstitute for Genetics, Justus-Liebig-University Giessen and Heinrich-Buff-Ring, 58-62 D-35392 Giessen, Germany.
Zihua Gong
Jörg Leers
Rainer Renkawitz
Justus-Liebig-Universität Gießen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Mi-2/NuRD complex is a multi-subunit protein complex with enzymatic activities involving chromatin remodeling and histone deacetylation. Targeting of Mi-2/NuRD to methylated CpG sequences mediates gene repression. The function of p66alpha and of p66beta within the multiple subunits has not been addressed. Here, we analyzed the in vivo function and binding of both p66-paralogs. Both factors function in synergy, since knocking-down p66alpha affects the repressive function of p66beta and vice versa. Both proteins interact with MBD2 functionally and biochemically. Mutation of a single amino acid of p66alpha abolishes in vivo binding to MBD2 and interferes with MBD2-mediated repression. This loss of binding results in a diffuse nuclear localization in contrast to wild-type p66alpha that shows a speckled nuclear distribution. Furthermore, wild-type subnuclear distribution of p66alpha and p66beta depends on the presence of MBD2. Both proteins interact with the tails of all octamer histones in vitro, and acetylation of histone tails interferes with p66 binding. The conserved region 2 of p66alpha is required for histone tail interaction as well as for wild-type subnuclear distribution. These results suggest a two-interaction forward feedback binding mode, with a stable chromatin association only after deacetylation of the histones has occurred.

Indexed as

AcetylationAnimalsCell LineCell NucleusDNA-Binding ProteinsGene SilencingHistone DeacetylasesHistonesHumansMi-2 Nucleosome Remodeling and Deacetylase ComplexMiceMutationProtein Structure, TertiaryRepressor ProteinsDNA-Binding ProteinsGATAD2A protein, humanGATAD2B protein, humanHistone DeacetylasesHistonesMBD2 proteinMbd2 protein, mouseMi-2 Nucleosome Remodeling and Deacetylase ComplexRepressor Proteins

Identifiers

PMID16415179
PMCPMC1331983
OpenAlexW2120277685

What Socratic 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 Socratic graph.