Evidence map›Paper›PMID 28827617›Full record

ArticleScientific reports2017

Glucocorticoid Receptor-mediated transactivation is hampered by Striatin-3, a novel interaction partner of the receptor.

Ioanna Petta, Nadia Bougarne, Jolien Vandewalle, Lien Dejager, Sofie Vandevyver, Marlies Ballegeer, Sofie Desmet, Jonathan Thommis, Lode De Cauwer, Sam Lievens and 3 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 24% 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

8 citing papers in PubMed, 10 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

13 authors at 3 institutions in 1 country.

Ioanna PettaReceptor Research Laboratories, Cytokine Receptor Lab, VIB, Center for Medical Biotechnology, Ghent, Belgium.
Nadia BougarneReceptor Research Laboratories, Cytokine Receptor Lab, VIB, Center for Medical Biotechnology, Ghent, Belgium.
Jolien VandewalleCenter for Inflammation Research, VIB, Ghent, Belgium.
Lien DejagerCenter for Inflammation Research, VIB, Ghent, Belgium.
Sofie VandevyverCenter for Inflammation Research, VIB, Ghent, Belgium.
Marlies BallegeerCenter for Inflammation Research, VIB, Ghent, Belgium.
Sofie DesmetReceptor Research Laboratories, Cytokine Receptor Lab, VIB, Center for Medical Biotechnology, Ghent, Belgium.
Jonathan ThommisReceptor Research Laboratories, Cytokine Receptor Lab, VIB, Center for Medical Biotechnology, Ghent, Belgium.
Lode De CauwerReceptor Research Laboratories, Cytokine Receptor Lab, VIB, Center for Medical Biotechnology, Ghent, Belgium.
Sam LievensReceptor Research Laboratories, Cytokine Receptor Lab, VIB, Center for Medical Biotechnology, Ghent, Belgium.
Claude LibertCenter for Inflammation Research, VIB, Ghent, Belgium.
Jan TavernierReceptor Research Laboratories, Cytokine Receptor Lab, VIB, Center for Medical Biotechnology, Ghent, Belgium.
Karolien De BosscherReceptor Research Laboratories, Cytokine Receptor Lab, VIB, Center for Medical Biotechnology, Ghent, Belgium. karolien.debosscher@vib-ugent.be.
Ghent University · BEVIB-UGent Center for Inflammation Research · BEVIB-UGent Center for Medical Biotechnology · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transcriptional activity of the glucocorticoid receptor (GR) is co-determined by its ability to recruit a vast and varying number of cofactors. We here identify Striatin-3 (STRN3) as a novel interaction partner of GR that interferes with GR's ligand-dependent transactivation capacity. Remarkably, STRN3 selectively affects only GR-dependent transactivation and leaves GR-dependent transrepression mechanisms unhampered. We found that STRN3 down-regulates GR transactivation by an additional recruitment of the catalytic subunit of protein phosphatase 2A (PPP2CA) to GR. We hypothesize the existence of a functional trimeric complex in the nucleus, able to dephosphorylate GR at serine 211, a known marker for GR transactivation in a target gene-dependent manner. The presence of STRN3 appears an absolute prerequisite for PPP2CA to engage in a complex with GR. Herein, the C-terminal domain of GR is essential, reflecting ligand-dependency, yet other receptor parts are also needed to create additional contacts with STRN3.

Indexed as

Down-RegulationA549 CellsAutoantigensBinding SitesCalmodulin-Binding ProteinsCell NucleusHEK293 CellsHeLa CellsHumansPhosphorylationProtein Interaction MapsProtein MultimerizationProtein Phosphatase 2Receptors, GlucocorticoidTranscriptional ActivationAutoantigensCalmodulin-Binding ProteinsPPP2CA protein, humanProtein Phosphatase 2Receptors, GlucocorticoidSTRN3 protein, human

Identifiers

PMID28827617
PMCPMC5567040
OpenAlexW2746965419

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.