Evidence map›Paper›PMID 32612187›Full record

ArticleScientific reports2020

Glucocorticoid receptor complexes form cooperatively with the Hsp90 co-chaperones Pp5 and FKBPs.

Anna Kaziales, Katalin Barkovits, Katrin Marcus, Klaus Richter

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. 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
1.8field-weighted citation impact, top 14% 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, 26 citations in OpenAlex.

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  16. Cortisol promotes stress tolerance via DAF-16 inBiochemistry and biophysics reports · 2021
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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

4 authors at 2 institutions in 1 country.

Anna KazialesCenter for Integrated Protein Science Munich at the Department of Chemistry, Technische Universität München, Lichtenbergstr. 4, 85748, Garching, Germany.
Katalin BarkovitsMedical Proteome Center, Ruhr University Bochum, Bochum, Germany.
Katrin MarcusMedical Proteome Center, Ruhr University Bochum, Bochum, Germany.
Klaus RichterCenter for Integrated Protein Science Munich at the Department of Chemistry, Technische Universität München, Lichtenbergstr. 4, 85748, Garching, Germany. klaus.richter@richterlab.de.
Center for Integrated Protein Science Munich · DERuhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The function of steroid receptors in the cell depends on the chaperone machinery of Hsp90, as Hsp90 primes steroid receptors for hormone binding and transcriptional activation. Several conserved proteins are known to additionally participate in receptor chaperone assemblies, but the regulation of the process is not understood in detail. Also, it is unknown to what extent the contribution of these cofactors is conserved in other eukaryotes. We here examine the reconstituted C. elegans and human chaperone assemblies. We find that the nematode phosphatase PPH-5 and the prolyl isomerase FKB-6 facilitate the formation of glucocorticoid receptor (GR) complexes with Hsp90. Within these complexes, Hsp90 can perform its closing reaction more efficiently. By combining chemical crosslinking and mass spectrometry, we define contact sites within these assemblies. Compared to the nematode Hsp90 system, the human system shows less cooperative client interaction and a stricter requirement for the co-chaperone p23 to complete the closing reaction of GR·Hsp90·Pp5/Fkbp51/Fkbp52 complexes. In both systems, hormone binding to GR is accelerated by Hsp90 alone and in the presence of its cofactors. Our results show that cooperative complex formation and hormone binding patterns are, in many aspects, conserved between the nematode and human systems.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsGlycoproteinsHSP90 Heat-Shock ProteinsHumansProtein BindingProtein Interaction Domains and MotifsReceptors, GlucocorticoidTacrolimus Binding ProteinsCaenorhabditis elegans ProteinsGlycoproteinsHSP90 Heat-Shock ProteinsReceptors, GlucocorticoidTacrolimus Binding Proteinstissue-factor-pathway inhibitor 2

Identifiers

PMID32612187
PMCPMC7329908
OpenAlexW3038856900

What OpenQuestion holds

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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.