Evidence map›Paper›PMID 34231305›Full record

ArticleThe FEBS journal2022

Unique protein interaction networks define the chromatin remodelling module of the NuRD complex.

Mehdi Sharifi Tabar, Caroline Giardina, Yue Feng, Habib Francis, Hakimeh Moghaddas Sani, Jason K K Low, Joel P Mackay, Charles G Bailey, John E J Rasko

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The FEBS journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

15 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Intrinsically Disordered Regions Define Unique Protein Interaction Networks in CHD Family Remodelers.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  4. The chromatin remodeler ADNP regulates neurodevelopmental disorder risk genes and neocortical neurogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Review
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 1 institution in 1 country.

Mehdi Sharifi TabarGene and Stem Cell Therapy Program Centenary Institute, The University of Sydney, Camperdown, NSW, Australia.
Caroline GiardinaGene and Stem Cell Therapy Program Centenary Institute, The University of Sydney, Camperdown, NSW, Australia.
Yue FengGene and Stem Cell Therapy Program Centenary Institute, The University of Sydney, Camperdown, NSW, Australia.
Habib FrancisGene and Stem Cell Therapy Program Centenary Institute, The University of Sydney, Camperdown, NSW, Australia.
Hakimeh Moghaddas SaniSchool of Life & Environmental Sciences, The University of Sydney, NSW, Australia.
Jason K K LowSchool of Life & Environmental Sciences, The University of Sydney, NSW, Australia.
Joel P MackaySchool of Life & Environmental Sciences, The University of Sydney, NSW, Australia.
Charles G BaileyGene and Stem Cell Therapy Program Centenary Institute, The University of Sydney, Camperdown, NSW, Australia.
John E J RaskoGene and Stem Cell Therapy Program Centenary Institute, The University of Sydney, Camperdown, NSW, Australia.ORCID 0000-0003-2975-807X
The University of Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The combination of four proteins and their paralogues including MBD2/3, GATAD2A/B, CDK2AP1 and CHD3/4/5, which we refer to as the MGCC module, form the chromatin remodelling module of the nucleosome remodelling and deacetylase (NuRD) complex. To date, mechanisms by which the MGCC module acquires paralogue-specific function and specificity have not been addressed. Understanding the protein-protein interaction (PPI) network of the MGCC subunits is essential for defining underlying mechanisms of gene regulation. Therefore, using pulldown followed by mass spectrometry analysis (PD-MS), we report a proteome-wide interaction network of the MGCC module in a paralogue-specific manner. Our data also demonstrate that the disordered C-terminal region of CHD3/4/5 is a gateway to incorporate remodelling activity into both ChAHP (CHD4, ADNP, HP1γ) and NuRD complexes in a mutually exclusive manner. We define a short aggregation-prone region (APR) within the C-terminal segment of GATAD2B that is essential for the interaction of CHD4 and CDK2AP1 with the NuRD complex. Finally, we also report an association of CDK2AP1 with the nuclear receptor co-repressor (NCOR) complex. Overall, this study provides insight into the possible mechanisms through which the MGCC module can achieve specificity and diverse biological functions.

Indexed as

Chromatin Assembly and DisassemblyDNA-Binding ProteinsDNA HelicasesGene Expression RegulationHumansMi-2 Nucleosome Remodeling and Deacetylase ComplexMultiprotein ComplexesNucleosomesProtein Interaction MapsProteomeRepressor ProteinsTumor Suppressor ProteinsCDK2AP1 protein, humanCHD3 protein, humanCHD4 protein, humanDNA-Binding ProteinsDNA HelicasesGATAD2A protein, humanMi-2 Nucleosome Remodeling and Deacetylase ComplexMultiprotein ComplexesNucleosomesProteomeRepressor ProteinsTumor Suppressor Proteinsaggregation prone regionChAHP complexCHD4chromatin remodellingNCOR complexNuRD complexprotein-protein interactions

Identifiers

PMID34231305
PMCPMC9545347
OpenAlexW3178813990

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.