Evidence map›Paper›PMID 11113208›Full record

ArticleMolecular and cellular biology2001

CIA, a novel estrogen receptor coactivator with a bifunctional nuclear receptor interacting determinant.

F Sauvé, L D McBroom, J Gallant, A N Moraitis, F Labrie, V Giguère

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.4field-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

32 citing papers in PubMed, 73 citations in OpenAlex.

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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 3 countries.

F SauvéMolecular Oncology Group, McGill University Health Centre, Montréal, Québec H3A 1A1.
L D McBroom
J Gallant
A N Moraitis
F Labrie
V Giguère
McGill University Health Centre · CALaval Mayenne Technopole · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coregulators for nuclear receptors (NR) are factors that either enhance or repress their transcriptional activity. Both coactivators and corepressors have been shown to use similar but functionally distinct NR interacting determinants containing the core motifs LxxLL and PhixxPhiPhi, respectively. These interactions occur through a hydrophobic cleft located on the surface of the ligand-binding domain (LBD) of the NR and are regulated by ligand-dependent activation function 2 (AF-2). In an effort to identify novel coregulators that function independently of AF-2, we used the LBD of the orphan receptor RVR (which lacks AF-2) as bait in a yeast two-hybrid screen. This strategy led to the cloning of a nuclear protein referred to as CIA (coactivator independent of AF-2 function) that possesses both repressor and activator functions. Strikingly, we observed that CIA not only interacts with RVR and Rev-ErbAalpha in a ligand-independent manner but can also form complexes with estrogen receptor alpha (ERalpha) and ERbeta in vitro and enhances ERalpha transcriptional activity in the presence of estradiol (E(2)). CIA-ERalpha interactions were found to be independent of AF-2 and enhanced by the antiestrogens EM-652 and ICI 182,780 but not by 4-hydroxytamoxifen and raloxifene. We further demonstrate that CIA-ERalpha interactions require the presence within CIA of a novel bifunctional NR recognition determinant containing overlapping LxxLL and PhixxPhiPhi motifs. The identification and functional characterization of CIA suggest that hormone binding can create a functional coactivator interaction interface in the absence of AF-2.

Indexed as

Gene Expression RegulationReceptors, Thyroid HormoneAmino Acid MotifsAmino Acid SequenceAnimalsBase SequenceBinding SitesCell LineCloning, MolecularEstrogen Receptor alphaGenes, ReporterHumansMicroscopy, FluorescenceMolecular Sequence DataNerve Tissue ProteinsNuclear ProteinsEstrogen Receptor alphaNCOA5 protein, humanNerve Tissue ProteinsNuclear ProteinsNuclear Receptor CoactivatorsReceptors, Cytoplasmic and NuclearReceptors, EstrogenReceptors, Thyroid HormoneRecombinant Fusion ProteinsRNA, MessengerSelective Estrogen Receptor ModulatorsTrans-ActivatorsTranscription Factors

Identifiers

PMID11113208
PMCPMC88807
OpenAlexW2060213573

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.