Evidence map›Paper›PMID 24753260›Full record

ArticleThe Journal of biological chemistry2014

The cochaperone SGTA (small glutamine-rich tetratricopeptide repeat-containing protein alpha) demonstrates regulatory specificity for the androgen, glucocorticoid, and progesterone receptors.

Atanu Paul, Yenni A Garcia, Bettina Zierer, Chaitanya Patwardhan, Omar Gutierrez, Zacariah Hildenbrand, Diondra C Harris, Heather A Balsiger, Jeffrey C Sivils, Jill L Johnson and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. 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
1.6field-weighted citation impact, top 17% 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, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Heat Shock Proteins in Benign Prostatic Hyperplasia and Prostate Cancer.International journal of molecular sciences · 2022
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. The roles of cytosolic quality control proteins, SGTA and the BAG6 complex, in disease.Advances in protein chemistry and structural biology · 2019
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
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 1 institution in 1 country.

Atanu PaulFrom the Border Biomedical Research Center and Department of Biological Sciences and.
Yenni A GarciaFrom the Border Biomedical Research Center and Department of Biological Sciences and.
Bettina Ziererthe Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Garching, Germany.
Chaitanya Patwardhanthe Cancer Research Center, Georgia Regents University, Augusta, Georgia 30912, and.
Omar GutierrezFrom the Border Biomedical Research Center and Department of Biological Sciences and.
Zacariah Hildenbrandthe Department of Chemistry, University of Texas at El Paso, El Paso, Texas 79968.
Diondra C HarrisFrom the Border Biomedical Research Center and Department of Biological Sciences and.
Heather A BalsigerFrom the Border Biomedical Research Center and Department of Biological Sciences and.
Jeffrey C SivilsFrom the Border Biomedical Research Center and Department of Biological Sciences and.
Jill L Johnsonthe Department of Biological Sciences, University of Idaho, Moscow, Idaho 83844.
Johannes Buchnerthe Center for Integrated Protein Science at the Department Chemie, Technische Universität München, Garching, Germany.
Ahmed Chadlithe Cancer Research Center, Georgia Regents University, Augusta, Georgia 30912, and.
Marc B CoxFrom the Border Biomedical Research Center and Department of Biological Sciences and mbcox@utep.edu.
Technical University of Munich · DE

Funding

TOXICOLOGY PROJECTG12RR008124 · NCRR · UNIVERSITY OF TEXAS EL PASO · PI WALSH, ELIZABETH J · 1992 to 2011
$20.8M
TCCG12MD007592 · NIMHD · UNIVERSITY OF TEXAS EL PASO · PI KIRKEN, ROBERT A. · 2012 to 2018
$19.4M
Functional Characterization of FKBP52 Interactions with Steroid Hormone ReceptorsSC1GM084863 · NIGMS · UNIVERSITY OF TEXAS EL PASO · PI COX, MARC B · 2008 to 2012
$1.2M
Targeting the core components of the Hsp90 chaperoning machineR01GM102443 · NIGMS · AUGUSTA UNIVERSITY · PI CHADLI, AHMED · 2012 to 2014
$743k
NCRR NIH HHS 5 G12 RR008124NCRR NIH HHS G12 RR008124NIGMS NIH HHS R01 GM102443NIGMS NIH HHS R01 GM102443-01NIGMS NIH HHS SC1 GM084863NIGMS NIH HHS SC1GM084863NIMHD NIH HHS 8 G12 MD007592NIMHD NIH HHS G12 MD007592
6 · The paper itself

Abstract

Steroid hormone receptors are ligand-dependent transcription factors that require the ordered assembly of multichaperone complexes for transcriptional activity. Although heat shock protein (Hsp) 90 and Hsp70 are key players in this process, multiple Hsp70- and Hsp90-associated cochaperones associate with receptor-chaperone complexes to regulate receptor folding and activation. Small glutamine-rich tetratricopeptide repeat-containing protein alpha (SGTA) was recently characterized as an Hsp70 and Hsp90-associated cochaperone that specifically regulates androgen receptor activity. However, the specificity of SGTA for additional members of the steroid hormone receptor superfamily and the mechanism by which SGTA regulates receptor activity remain unclear. Here we report that SGTA associates with and specifically regulates the androgen, glucocorticoid, and progesterone receptors and has no effect on the mineralocorticoid and estrogen receptors in both yeast and mammalian cell-based reporter assays. In both systems, SGTA knockdown/deletion enhances receptor activity, whereas SGTA overexpression suppresses receptor activity. We demonstrate that SGTA binds directly to Hsp70 and Hsp90 in vitro with similar affinities yet predominately precipitates with Hsp70 from cell lysates, suggesting a role for SGTA in early, Hsp70-mediated folding. Furthermore, SGTA expression completely abrogates the regulation of receptor function by FKBP52 (52-kDa FK506-binding protein), which acts at a later stage of the chaperone cycle. Taken together, our data suggest a role for SGTA at distinct steps in the chaperone-dependent modulation of androgen, glucocorticoid, and progesterone receptor activity.

Indexed as

Amino Acid SequenceCarrier ProteinsGene Knockdown TechniquesHeLa CellsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansMolecular ChaperonesMolecular Sequence DataReceptors, AndrogenReceptors, GlucocorticoidReceptors, ProgesteroneSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTacrolimus Binding ProteinsTwo-Hybrid System TechniquesCarrier ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesReceptors, AndrogenReceptors, GlucocorticoidReceptors, ProgesteroneSaccharomyces cerevisiae ProteinsSgt2 protein, S cerevisiaeSGTA protein, humantacrolimus binding protein 4Tacrolimus Binding ProteinsAndrogen ReceptorCochaperoneFKBP52Glucocorticoid ReceptorHeat Shock Protein 90 (Hsp90)Hsp70ProgesteroneProstate CancerSGTASteroid Hormone Receptor

Identifiers

PMID24753260
PMCPMC4140887
OpenAlexW2105272991

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.