Evidence map›Paper›PMID 11027271›Full record

ArticleMolecular and cellular biology2000

Discrete roles for peroxisome proliferator-activated receptor gamma and retinoid X receptor in recruiting nuclear receptor coactivators.

W Yang, C Rachez, L P Freedman

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

41 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
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

3 authors at 1 institution in 1 country.

W YangCell Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
C Rachez
L P Freedman
Memorial Sloan Kettering Cancer Center · US

Funding

ENDOCRINE RESEARCH TRAINING PROGRAMT32DK007313 · NIDDK · WEILL MEDICAL COLL OF CORNELL UNIV · PI IMPERATO-MCGINLEY, JULIANNE L · 1986 to 2011
$1.9M
VITAMIN D3-INDUCIBLE GENES MEDIATING DIFFERENTIATIONR01DK052621 · NIDDK · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI NIMER, STEPHEN DAVID · 1997 to 2004
$1.4M
MECHANISMS OF GENE CONTROL BY THE VITAMIN D3 RECEPTORR01DK045460 · NIDDK · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI FISHER, ROBERT P · 1992 to 2004
$874k
MECHANISMS OF GENE CONTROL BY THE VITAMIN D3 RECEPTORR37DK045460 · NIDDK · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI FREEDMAN, LEONARD P · 2000 to 2001
$583k
NIDDK NIH HHS DK07313NIDDK NIH HHS DK45460NIDDK NIH HHS DK52621NIDDK NIH HHS R01 DK045460NIDDK NIH HHS R01 DK052621NIDDK NIH HHS R37 DK045460NIDDK NIH HHS T32 DK007313
6 · The paper itself

Abstract

Peroxisome proliferator-activated receptor gamma (PPARgamma) plays a major role in adipogenesis. PPARgamma binds to DNA as a heterodimer with retinoid X receptor (RXR), and PPARgamma-RXR can be activated by ligands specific for either receptor; the presence of both ligands can result in a cooperative effect on the transactivation of target genes. How these ligands mediate transactivation, however, remains unclear. PPARgamma is known to interact with both the p160/SRC-1 family of coactivators and the distinct, multisubunit coactivator complex called DRIP. A single DRIP subunit, DRIP205 (TRAP220, PBP), binds directly to PPARgamma. Here we report that PPARgamma and RXR selectively interacted with DRIP205 and p160 proteins in a ligand-dependent manner. At physiological concentrations, RXR-specific ligands only induced p160 binding to RXR, and PPARgamma-specific ligands exclusively recruited DRIP205 but not p160 coactivators to PPARgamma. This selectivity was not observed in interaction assays off DNA, implying that the specificity of coactivator binding in response to ligand is strongly influenced by the allosteric effects of DNA-bound heterodimers. These coactivator-selective effects were also observed in transient-transfection assays in the presence of overexpressed p160 or DRIP coactivators. The results suggest that the cooperative effects of PPARgamma- and RXR-specific ligands may occur at the level of selective coactivator recruitment.

Indexed as

3T3 CellsAnimalsCarrier ProteinsCell LineCell NucleusDimerizationDose-Response Relationship, DrugGlutathione TransferaseHistone AcetyltransferasesLigandsMediator Complex Subunit 1MiceModels, BiologicalNuclear Receptor Coactivator 1Protein BindingReceptors, Cytoplasmic and NuclearCarrier ProteinsGlutathione TransferaseHistone AcetyltransferasesLigandsMed1 protein, mouseMediator Complex Subunit 1Ncoa1 protein, mouseNuclear Receptor Coactivator 1Receptors, Cytoplasmic and NuclearReceptors, Retinoic AcidRecombinant Fusion ProteinsRetinoid X ReceptorsTranscription Factors

Identifiers

PMID11027271
PMCPMC86411
OpenAlexW2142047562

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.