Evidence map›Paper›PMID 33790284›Full record

ArticleNature communications2021

Genome-wide binding potential and regulatory activity of the glucocorticoid receptor's monomeric and dimeric forms.

Thomas A Johnson, Ville Paakinaho, Sohyoung Kim, Gordon L Hager, Diego M Presman

Abstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
–field-weighted citation impact
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

45 citing papers in PubMed.

  1. Review
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  17. The glucocorticoid receptor potentiates aldosterone-induced transcription by the mineralocorticoid receptor.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
  19. Article
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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

5 authors.

Thomas A Johnson *Laboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Building 41, 41 Library Drive, Bethesda, MD, USA.
Ville Paakinaho *Laboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Building 41, 41 Library Drive, Bethesda, MD, USA.ORCID http://orcid.org/0000-0003-4204-1436
Sohyoung KimLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Building 41, 41 Library Drive, Bethesda, MD, USA.ORCID http://orcid.org/0000-0002-6140-7918
Gordon L HagerLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Building 41, 41 Library Drive, Bethesda, MD, USA. hagerg@exchange.nih.gov.ORCID http://orcid.org/0000-0002-9300-5331
Diego M PresmanLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Building 41, 41 Library Drive, Bethesda, MD, USA. presmandm@fbmc.fcen.uba.ar.ORCID http://orcid.org/0000-0003-4515-8058

Funding

Chromatin Structure and Gene ExpressionZIABC005450 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HAGER, GORDON L · 2009 to 2025
$35.2M
Chromatin Remodeling ProteinsZIABC010646 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HAGER, GORDON L · 2009 to 2021
$4.0M
6 · The paper itself

Abstract

A widely regarded model for glucocorticoid receptor (GR) action postulates that dimeric binding to DNA regulates unfavorable metabolic pathways while monomeric receptor binding promotes repressive gene responses related to its anti-inflammatory effects. This model has been built upon the characterization of the GRdim mutant, reported to be incapable of DNA binding and dimerization. Although quantitative live-cell imaging data shows GRdim as mostly dimeric, genomic studies based on recovery of enriched half-site response elements suggest monomeric engagement on DNA. Here, we perform genome-wide studies on GRdim and a constitutively monomeric mutant. Our results show that impairing dimerization affects binding even to open chromatin. We also find that GRdim does not exclusively bind half-response elements. Our results do not support a physiological role for monomeric GR and are consistent with a common mode of receptor binding via higher order structures that drives both the activating and repressive actions of glucocorticoids.

Indexed as

Protein MultimerizationAnimalsChromatinDNAGene Expression RegulationGenome-Wide Association StudyGlucocorticoidsHumansMiceMutationProtein BindingReceptors, GlucocorticoidResponse ElementsSignal TransductionChromatinDNAGlucocorticoidsReceptors, Glucocorticoid

Identifiers

PMID33790284
PMCPMC8012360

What Socratic holds

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Registered trials

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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.