Evidence map›Paper›PMID 10947077›Full record

ArticleGene expression1999

Nuclear receptor coactivator SRC-1 interacts with the Q-rich subdomain of the AhR and modulates its transactivation potential.

M B Kumar, G H Perdew

Open access · greenAbstract read
In one paragraph

Article in Gene expression, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.2field-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

42 citing papers in PubMed, 113 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. The Landscape of AhR Regulators and Coregulators to Fine-Tune AhR Functions.International journal of molecular sciences · 2021
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Coactivator recruitment of AhR/ARNT1.International journal of molecular sciences · 2014
    Review
  19. bHLH-PAS proteins in cancer.Nature reviews. Cancer · 2013
    Review
  20. Role of the aryl hydrocarbon receptor in carcinogenesis and potential as a drug target.Toxicological sciences : an official journal of the Society of Toxicology · 2013
    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

2 authors at 1 institution in 2 countries.

M B KumarGraduate Program in Biochemistry and Molecular Biology, The Pennsylvania State University, University Park 16802, USA.
G H Perdew
Pennsylvania State University · US

Funding

REGULATION OF THE AH RECEPTORR01ES004869 · NIEHS · PURDUE UNIVERSITY WEST LAFAYETTE · PI PERDEW, GARY H. · 1994 to 2017
$5.3M
BIOCHEMICAL CHARACTERIZATION OF THE AH RECEPTORR29ES004869 · NIEHS · PURDUE UNIVERSITY WEST LAFAYETTE · PI PERDEW, GARY H · 1989 to 1993
–
NIEHS NIH HHS ES 04869NIEHS NIH HHS R01 ES004869
6 · The paper itself

Abstract

The aryl hydrocarbon receptor (AhR), a soluble cytosolic protein, mediates many of the toxic effects of TCDD and related chemicals. The toxic effects are largely cell, tissue, and promoter context dependent. Although many details of the overall dioxin signal transduction have been elucidated, the transcriptional regulation of dioxin-induced genes like cyp1A1 is not yet completely understood. Previously, we have shown that the co-regulator RIP140 is a potential AhR coactivator. In this report, the role of coactivator, SRC-1, in AhR-mediated transcriptional regulation was examined. SRC-1 increased AhR-mediated, TCDD-dependent reporter gene activity three-fold in Hepa-1 and COS-1 cells. In in vitro interaction assays, SRC-1 was found to interact with AhR but not with ARNT. SRC-1 interacted weakly with AhR in the absence of TCDD and the addition of ligand further increased SRC-1 binding to AhR. Deletional mapping studies of the AhR revealed that SRC-1 binds to the AhR transactivation domain. Finer mapping of the SRC-1-interacting subdomains in the AhR transactivation domain suggested that the Q-rich subdomain was necessary and sufficient for interaction, similar to that seen with RIP140. Using GFP-tagged constructs, SRC-1 was shown to interact with AhR in cells. Unlike RIP140, LXXLL motifs in SRC-1 were necessary for interaction with AhR in vitro and for coactivation in Hepa-1 cells. The recruitment of certain coactivators by a variety of receptors suggests possible common coactivator pools and competition among receptors for limiting coactivators. Examination of the role of SRC-1 in AhR/ARNT transactivation in ARNT-deficient mutant Hepa-1 c4 cells demonstrates that the AhR transactivation domain is sufficient for enhanced coactivation mediated by SRC-1 in the presence of a transactivation domain deleted ARNT protein.

Indexed as

DNA-Binding ProteinsTranscriptional ActivationAdaptor Proteins, Signal TransducingAmino Acid MotifsAnimalsAryl Hydrocarbon Receptor Nuclear TranslocatorBinding SitesCell LineCOS CellsGreen Fluorescent ProteinsHistone AcetyltransferasesHumansLuminescent ProteinsMutationNuclear ProteinsNuclear Receptor Coactivator 1Adaptor Proteins, Signal TransducingARNT protein, humanAryl Hydrocarbon Receptor Nuclear TranslocatorDNA-Binding ProteinsGreen Fluorescent ProteinsHistone AcetyltransferasesLuminescent ProteinsNCOA1 protein, humanNRIP1 protein, humanNuclear ProteinsNuclear Receptor Coactivator 1Nuclear Receptor Interacting Protein 1Polychlorinated DibenzodioxinsReceptors, Aryl HydrocarbonRecombinant ProteinsTranscription Factors

Identifiers

PMID10947077
PMCPMC6157383
OpenAlexW2416977311

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.