Evidence map›Paper›PMID 27382178›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

DNA binding triggers tetramerization of the glucocorticoid receptor in live cells.

Diego M Presman, Sourav Ganguly, R Louis Schiltz, Thomas A Johnson, Tatiana S Karpova, Gordon L Hager

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed, 1 pooled it
–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

86 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  12. Corticosteroids in sepsis.Journal of intensive medicine · 2025
    Review
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26 more citing papers are in PubMed but not listed here.

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

6 authors.

Diego M PresmanLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Bethesda, MD 20892 presmandm@mail.nih.gov hagerg@exchange.nih.gov.
Sourav GangulyLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Bethesda, MD 20892.
R Louis SchiltzLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Bethesda, MD 20892.
Thomas A JohnsonLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Bethesda, MD 20892.
Tatiana S KarpovaLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Bethesda, MD 20892.
Gordon L HagerLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Bethesda, MD 20892 presmandm@mail.nih.gov hagerg@exchange.nih.gov.

Funding

Transcription factor mobilityZICBC011571 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI KARPOVA, TATIANA · 2014 to 2025
$3.0M
6 · The paper itself

Abstract

Transcription factors dynamically bind to chromatin and are essential for the regulation of genes. Although a large percentage of these proteins appear to self-associate to form dimers or higher order oligomers, the stoichiometry of DNA-bound transcription factors has been poorly characterized in vivo. The glucocorticoid receptor (GR) is a ligand-regulated transcription factor widely believed to act as a dimer or a monomer. Using a unique set of imaging techniques coupled with a cell line containing an array of DNA binding elements, we show that GR is predominantly a tetramer when bound to its target DNA. We find that DNA binding triggers an interdomain allosteric regulation within the GR, leading to tetramerization. We therefore propose that dynamic changes in GR stoichiometry represent a previously unidentified level of regulation in steroid receptor activation. Quaternary structure analysis of other members of the steroid receptor family (estrogen, androgen, and progesterone receptors) reveals variation in oligomerization states among this family of transcription factors. Because GR's oligomerization state has been implicated in therapy outcome, our findings open new doors to the rational design of novel GR ligands and redefine the quaternary structure of steroid receptors.

Indexed as

AnimalsCell Line, TumorCells, CulturedDNAFibroblastsMice, KnockoutProtein MultimerizationReceptors, GlucocorticoidDNAReceptors, Glucocorticoiddimerglucocorticoid receptornumber and brightnesssteroid receptorstetramer

Identifiers

PMID27382178
PMCPMC4961135

What OpenQuestion 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 OpenQuestion graph.