Evidence map›Paper›PMID 12754377›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

The basic helix-loop-helix-PAS protein ARNT functions as a potent coactivator of estrogen receptor-dependent transcription.

Sara Brunnberg, Katarina Pettersson, Elin Rydin, Jason Matthews, Annika Hanberg, Ingemar Pongratz

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

59 citing papers in PubMed, 147 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. bHLH-PAS Proteins: Their Structure and Intrinsic Disorder.International journal of molecular sciences · 2019
    Review
  9. Article
  10. Article
  11. Crosstalk between Notch, HIF-1α and GPER in Breast Cancer EMT.International journal of molecular sciences · 2018
    Review
  12. Review
  13. Adipose Tissue as a Site of Toxin Accumulation.Comprehensive Physiology · 2017
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Coactivator recruitment of AhR/ARNT1.International journal of molecular sciences · 2014
    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

6 authors at 2 institutions in 2 countries.

Sara BrunnbergDepartment of Cell and Molecular Biology, Karolinska Institutet, S-171 77 Stockholm, Sweden.
Katarina Pettersson
Elin Rydin
Jason Matthews
Annika Hanberg
Ingemar Pongratz
Karolinska Institutet · SEInstitute of Molecular and Cell Biology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biological effects of estrogens are mediated by the estrogen receptors ERalpha and ERbeta. These receptors regulate gene expression through binding to DNA enhancer elements and subsequently recruiting factors such as coactivators that modulate their transcriptional activity. Here we show that ARNT (aryl hydrocarbon receptor nuclear translocator), the obligatory heterodimerization partner for the aryl hydrocarbon receptor and hypoxia inducible factor 1alpha, functions as a potent coactivator of ERalpha- and ERbeta- dependent transcription. The coactivating effect of ARNT depends on physical interaction with the ERs and involves the C-terminal domain of ARNT and not the structurally conserved basic helix-loop-helix and PAS (Per-ARNT-Sim) motifs. Moreover, we show that ARNT/ER interaction requires the E2-activated ligand binding domain of ERalpha or ERbeta. These observations, together with the previous role of ARNT as an obligatory partner protein for conditionally regulated basic helix-loop-helix-PAS proteins like the aryl hydrocarbon receptor or hypoxia inducible factor 1alpha, expand the cellular functions of ARNT to include regulation of ERalpha and ERbeta transcriptional activity. ARNT was furthermore recruited to a natural ER target gene promoter in a estrogen-dependent manner, supporting a physiological role for ARNT as an ER coactivator.

Indexed as

DNA-Binding ProteinsHelix-Loop-Helix MotifsReceptors, Aryl HydrocarbonAnimalsAryl Hydrocarbon Receptor Nuclear TranslocatorCOS CellsEstrogen Receptor alphaEstrogen Receptor betaHeLa CellsHumansPrecipitin TestsPromoter Regions, GeneticReceptors, EstrogenTranscription FactorsARNT protein, humanAryl Hydrocarbon Receptor Nuclear TranslocatorDNA-Binding ProteinsEstrogen Receptor alphaEstrogen Receptor betaReceptors, Aryl HydrocarbonReceptors, EstrogenTranscription Factors

Identifiers

PMID12754377
PMCPMC164478
OpenAlexW1982395222

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.