Evidence map›Paper›PMID 20048054›Full record

ArticleMolecular and cellular biology2010

FKBP51 promotes assembly of the Hsp90 chaperone complex and regulates androgen receptor signaling in prostate cancer cells.

Li Ni, Chun-Song Yang, Daniel Gioeli, Henry Frierson, David O Toft, Bryce M Paschal

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed, 1 pooled it
6.0field-weighted citation impact, top 3% 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

89 citing papers in PubMed, 1 synthesis or guideline pooled it, 155 citations in OpenAlex.

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  17. 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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29 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Li NiCenter for Cell Signaling, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA.
Chun-Song Yang
Daniel Gioeli
Henry Frierson
David O Toft
Bryce M Paschal
Toxicologie, Pharmacologie et Signalisation Cellulaire · FRMayo Clinic · USUniversity of Virginia · US

Funding

VEGF, FAK and RAPP01CA104106 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI PASCHAL, BRYCE, THEODORESCU, DAN · 2005 to 2015
$17.9M
Role of Androgen Receptor Phosphorylation in Prostate CancerR01CA124706 · NCI · UNIVERSITY OF VIRGINIA · PI GIOELI, DANIEL G · 2008 to 2012
$1.6M
NCI NIH HHS P01 CA104106NCI NIH HHS P01-CA104106NCI NIH HHS R01 CA124706
6 · The paper itself

Abstract

Prostate cancer progression to the androgen-independent (AI) state involves acquisition of pathways that allow tumor growth under low-androgen conditions. We hypothesized that expression of molecular chaperones that modulate androgen binding to AR might be altered in prostate cancer and contribute to progression to the AI state. Here, we report that the Hsp90 cochaperone FKBP51 is upregulated in LAPC-4 AI tumors grown in castrated mice and describe a molecular mechanism by which FKBP51 regulates AR activity. Using recombinant proteins, we show that FKBP51 stimulates recruitment of the cochaperone p23 to the ATP-bound form of Hsp90, forming an FKBP51-Hsp90-p23 superchaperone complex. In cells, FKBP51 expression promotes superchaperone complex association with AR and increases the number of AR molecules that undergo androgen binding. FKBP51 stimulates androgen-dependent transcription and cell growth, and FKBP51 is part of a positive feedback loop that is regulated by AR and androgen. Finally, depleting FKBP51 levels by short hairpin RNA reduces the transcript levels of genes regulated by AR and androgen. Because the superchaperone complex plays a critical role in determining the ligand-binding competence and transcription function of AR, it provides an attractive target for inhibiting AR activity in prostate cancer cells.

Indexed as

AnimalsBase SequenceCell Line, TumorDNA PrimersHSP90 Heat-Shock ProteinsHumansIntramolecular OxidoreductasesMaleMiceMice, SCIDModels, BiologicalMultiprotein ComplexesNeoplasms, Hormone-DependentNeoplasm TransplantationProstaglandin-E SynthasesProstatic NeoplasmsAR protein, humanDNA PrimersHSP90 Heat-Shock ProteinsIntramolecular OxidoreductasesMultiprotein ComplexesProstaglandin-E SynthasesReceptors, AndrogenRecombinant ProteinsTacrolimus Binding Protein 5Tacrolimus Binding Proteins

Identifiers

PMID20048054
PMCPMC2820886
OpenAlexW2059122555

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.