Evidence map›Paper›PMID 24642507›Full record

ArticlePLoS biology2014

Live cell imaging unveils multiple domain requirements for in vivo dimerization of the glucocorticoid receptor.

Diego M Presman, M Florencia Ogara, Martín Stortz, Lautaro D Alvarez, John R Pooley, R Louis Schiltz, Lars Grøntved, Thomas A Johnson, Paul R Mittelstadt, Jonathan D Ashwell and 5 more

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
11.2field-weighted citation impact, top 1% 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

73 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. The mineralocorticoid receptor forms higher order oligomers upon DNA binding.Protein science : a publication of the Protein Society · 2024
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Structural insights into glucocorticoid receptor function.Biochemical Society transactions · 2021
    Review

13 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 6 institutions in 3 countries.

Diego M PresmanLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Bethesda, Maryland, United States of America; Department of Biological Chemistry, School of Sciences (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina; IFIBYNE-CONICET, School of Sciences (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina.
M Florencia OgaraDepartment of Biological Chemistry, School of Sciences (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina; IFIBYNE-CONICET, School of Sciences (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina.
Martín StortzDepartment of Biological Chemistry, School of Sciences (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina.
Lautaro D AlvarezDepartment of Organic Chemistry/UMYMFOR-CONICET, School of Sciences (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina.
John R PooleyLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Bethesda, Maryland, United States of America; Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology, University of Bristol, Bristol, United Kingdom.
R Louis SchiltzLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Bethesda, Maryland, United States of America.
Lars GrøntvedLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Bethesda, Maryland, United States of America.
Thomas A JohnsonLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Bethesda, Maryland, United States of America.
Paul R MittelstadtLaboratory of Immune Cell Biology, Center for Cancer Research, National Cancer Institute, Bethesda, Maryland, United States of America.
Jonathan D AshwellLaboratory of Immune Cell Biology, Center for Cancer Research, National Cancer Institute, Bethesda, Maryland, United States of America.
Sundar GanesanBiological Imaging Section, Research Technologies Branch, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland, United States of America.
Gerardo BurtonDepartment of Organic Chemistry/UMYMFOR-CONICET, School of Sciences (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina.
Valeria LeviDepartment of Biological Chemistry, School of Sciences (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina.
Gordon L HagerLaboratory of Receptor Biology and Gene Expression, National Cancer Institute, NIH, Bethesda, Maryland, United States of America.
Adali PecciDepartment of Biological Chemistry, School of Sciences (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina; IFIBYNE-CONICET, School of Sciences (FCEN), University of Buenos Aires (UBA), Buenos Aires, Argentina.
University of Buenos Aires · ARNational Institutes of Health · USConsejo Nacional de Investigaciones Científicas y Técnicas · ARNational Cancer Institute · USCenter for Cancer Research · USNational Institute of Allergy and Infectious Diseases · US

Funding

LRBGE Optical Microscopy CoreZICBC011574 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI KARPOVA, TATIANA · 2014 to 2025
$7.4M
Intramural NIH HHS
6 · The paper itself

Abstract

Glucocorticoids are essential for life, but are also implicated in disease pathogenesis and may produce unwanted effects when given in high doses. Glucocorticoid receptor (GR) transcriptional activity and clinical outcome have been linked to its oligomerization state. Although a point mutation within the GR DNA-binding domain (GRdim mutant) has been reported as crucial for receptor dimerization and DNA binding, this assumption has recently been challenged. Here we have analyzed the GR oligomerization state in vivo using the number and brightness assay. Our results suggest a complete, reversible, and DNA-independent ligand-induced model for GR dimerization. We demonstrate that the GRdim forms dimers in vivo whereas adding another mutation in the ligand-binding domain (I634A) severely compromises homodimer formation. Contrary to dogma, no correlation between the GR monomeric/dimeric state and transcriptional activity was observed. Finally, the state of dimerization affected DNA binding only to a subset of GR binding sites. These results have major implications on future searches for therapeutic glucocorticoids with reduced side effects.

Indexed as

AnimalsCells, CulturedDNAMiceProtein MultimerizationProtein Structure, TertiaryReceptors, GlucocorticoidDNAReceptors, Glucocorticoid

Identifiers

PMID24642507
PMCPMC3958349
OpenAlexW2045008807

What OpenQuestion holds

Textmetadata
LicenceCC0
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.