Evidence map›Paper›PMID 20661446›Full record

ArticlePloS one2010

Differential impact of tetratricopeptide repeat proteins on the steroid hormone receptors.

Jan-Philip Schülke, Gabriela Monika Wochnik, Isabelle Lang-Rollin, Nils Christian Gassen, Regina Theresia Knapp, Barbara Berning, Alexander Yassouridis, Theo Rein

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed, 108 citations in OpenAlex.

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  11. FKBP52 and FKBP51 differentially regulate the stability of estrogen receptor in breast cancer.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  12. DnaJC7 in Amyotrophic Lateral Sclerosis.International journal of molecular sciences · 2022
    Review
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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

8 authors at 2 institutions in 1 country.

Jan-Philip SchülkeChaperone Research Group, Max Planck Institute of Psychiatry, Munich, Germany.
Gabriela Monika Wochnik
Isabelle Lang-Rollin
Nils Christian Gassen
Regina Theresia Knapp
Barbara Berning
Alexander Yassouridis
Theo Rein
Max Planck Institute of Psychiatry · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundTetratricopeptide repeat (TPR) motif containing co-chaperones of the chaperone Hsp90 are considered control modules that govern activity and specificity of this central folding platform. Steroid receptors are paradigm clients of Hsp90. The influence of some TPR proteins on selected receptors has been described, but a comprehensive analysis of the effects of TPR proteins on all steroid receptors has not been accomplished yet. METHODOLOGY AND PRINCIPAL

findingsWe compared the influence of the TPR proteins FK506 binding proteins 51 and 52, protein phosphatase-5, C-terminus of Hsp70 interacting protein, cyclophillin 40, hepatitis-virus-B X-associated protein-2, and tetratricopeptide repeat protein-2 on all six steroid hormone receptors in a homogeneous mammalian cell system. To be able to assess each cofactor's effect on the transcriptional activity of on each steroid receptor we employed transient transfection in a reporter gene assay. In addition, we evaluated the interactions of the TPR proteins with the receptors and components of the Hsp90 chaperone heterocomplex by coimmunoprecipitation. In the functional assays, corticosteroid and progesterone receptors displayed the most sensitive and distinct reaction to the TPR proteins. Androgen receptor's activity was moderately impaired by most cofactors, whereas the Estrogen receptors' activity was impaired by most cofactors only to a minor degree. Second, interaction studies revealed that the strongly receptor-interacting co-chaperones were all among the inhibitory proteins. Intriguingly, the TPR-proteins also differentially co-precipitated the heterochaperone complex components Hsp90, Hsp70, and p23, pointing to differences in their modes of action. CONCLUSION AND SIGNIFICANCE: The results of this comprehensive study provide important insight into chaperoning of diverse client proteins via the combinatorial action of (co)-chaperones. The differential effects of the TPR proteins on steroid receptors bear on all physiological processes related to steroid hormone activity.

Indexed as

AnimalsCell LineCell Line, TumorCyclophilinsHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHumansImmunoblottingImmunoprecipitationIntracellular Signaling Peptides and ProteinsMiceMolecular ChaperonesNuclear ProteinsPeptidyl-Prolyl Isomerase FPhosphoprotein PhosphatasesReceptors, Androgenaryl hydrocarbon receptor-interacting proteinCyclophilinsDNAJC7 protein, humanHeat-Shock ProteinsHSP40 Heat-Shock ProteinsIntracellular Signaling Peptides and ProteinsMolecular ChaperonesNuclear ProteinsPeptidyl-Prolyl Isomerase FPhosphoprotein PhosphatasesPPIF protein, mouseprotein phosphatase 5Receptors, AndrogenReceptors, EstrogenReceptors, GlucocorticoidReceptors, MineralocorticoidReceptors, ProgesteroneReceptors, SteroidSTUB1 protein, humanTacrolimus Binding ProteinsUbiquitin-Protein Ligases

Identifiers

PMID20661446
PMCPMC2908686
OpenAlexW1991246477

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.