Evidence map›Paper›PMID 23887939›Full record

ArticleNucleic acids research2013

Pin1 promotes GR transactivation by enhancing recruitment to target genes.

Toryn M Poolman, Stuart N Farrow, Laura Matthews, Andrew S Loudon, David W Ray

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

19 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
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  9. Nuclear receptor REVERBα is a state-dependent regulator of liver energy metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Pinning Down the Transcription: A Role for Peptidyl-ProlylFrontiers in cell and developmental biology · 2020
    Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
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  18. Glucocorticoid receptor regulates accurate chromosome segregation and is associated with malignancy.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. 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

5 authors at 2 institutions in 1 country.

Toryn M PoolmanCentre in Endocrinology and Diabetes, Institute of Human Development, University of Manchester, Manchester, M13 9PT, UK, Respiratory Therapy Area, GSK, Stevenage, SG1 2NY, UK, Faculty of Life Sciences, University of Manchester, Manchester, M13 9PT, UK and Manchester Academic Health Sciences Centre, Manchester M13 9NT, UK.
Stuart N Farrow
Laura Matthews
Andrew S Loudon
David W Ray
Manchester Academic Health Science Centre · GBUniversity of Manchester · GB

Funding

Wellcome Trust 097820
6 · The paper itself

Abstract

The glucocorticoid receptor (GR) is a ligand activated transcription factor, serving to regulate both energy metabolism and immune functions. Factors that influence cellular sensitivity to glucocorticoids (GC) are therefore of great interest. The N-terminal of the GR contains numerous potential proline-directed phosphorylation sites, some of which can regulate GR transactivation. Unrestricted proline isomerisation can be inhibited by adjacent serine phosphorylation and requires a prolyl isomerise, Pin1. Pin1 therefore determines the functional outcome of proline-directed kinases acting on the GR, as cis/trans isomers are distinct pools with different interacting proteins. We show that Pin1 mediates GR transactivation, but not GR trans-repression. Two N-terminal GR serines, S203 and S211, are targets for Pin1 potentiation of GR transactivation, establishing a direct link between Pin1 and the GR. We also demonstrate GC-activated co-recruitment of GR and Pin1 to the GILZ gene promoter. The Pin1 effect required both its WW and catalytic domains, and GR recruitment to its GRE was Pin1-dependent. Therefore, Pin1 is a selective regulator of GR transactivation, acting through N-terminal phospho-serine residues to regulate GR recruitment to its target sites in the genome. As Pin1 is dysregulated in disease states, this interaction may contribute to altered GC action in inflammatory conditions.

Indexed as

Transcriptional ActivationCell LineDexamethasoneHumansNIMA-Interacting Peptidylprolyl IsomeraseNuclear Receptor Coactivator 3Peptidylprolyl IsomerasePhosphorylationPromoter Regions, GeneticProtein StabilityReceptors, GlucocorticoidRepressor ProteinsDexamethasoneNIMA-Interacting Peptidylprolyl IsomeraseNuclear Receptor Coactivator 3Peptidylprolyl IsomerasePIN1 protein, humanReceptors, GlucocorticoidRepressor Proteins

Identifiers

PMID23887939
PMCPMC3794586
OpenAlexW2149043457

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.