Evidence map›Paper›PMID 20038533›Full record

ArticleMolecular and cellular biology2010

The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events.

Mario D Galigniana, Alejandra G Erlejman, Martín Monte, Celso Gomez-Sanchez, Graciela Piwien-Pilipuk

Open access · bronzeAbstract 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 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

63 citing papers in PubMed, 148 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. FKBP51 and the molecular chaperoning of metabolism.Trends in endocrinology and metabolism: TEM · 2021
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review

3 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

5 authors at 3 institutions in 2 countries.

Mario D GalignianaInstituto de Biología y Medicina Experimental/CONICET, Buenos Aires, Argentina.
Alejandra G Erlejman
Martín Monte
Celso Gomez-Sanchez
Graciela Piwien-Pilipuk
Fundación Ciencias Exactas y Naturales · ARExperimental Medicine and Biology Institute · ARG.V. (Sonny) Montgomery VA Medical Center · US

Funding

ROLE OF MINERALOCORTICOIDS IN LOW-RENIN HYPERTENSIONR01HL027255 · NHLBI · UNIVERSITY OF SOUTH FLORIDA · PI GOMEZ-SANCHEZ, CELSO ENRIQUE · 1985 to 2017
$3.9M
Chaperones, immunophilins and nuclear receptor shuttlingR03TW007162 · FIC · UNIVERSITY OF MISSISSIPPI MED CTR · PI GOMEZ-SANCHEZ, CELSO ENRIQUE · 2007 to 2009
$107k
C/EBPb and heterochromatin: their role in adipogenesisR03TW008143 · FIC · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHWARTZ, JESSICA · 2009 to 2011
$103k
FIC NIH HHS R03 TW007162FIC NIH HHS R03TW007162-01A2FIC NIH HHS R03 TW008143FIC NIH HHS R03TW008143-01A1NHLBI NIH HHS R01 HL027255
6 · The paper itself

Abstract

In this study, we demonstrate that the subcellular localization of the mineralocorticoid receptor (MR) is regulated by tetratricopeptide domain (TPR) proteins. The high-molecular-weight immunophilin (IMM) FKBP52 links the MR-hsp90 complex to dynein/dynactin motors favoring the cytoplasmic transport of MR to the nucleus. Replacement of this hsp90-binding IMM by FKBP51 or the TPR peptide favored the cytoplasmic localization of MR. The complete movement machinery, including dynein and tubulin, could be recovered from paclitaxel/GTP-stabilized cytosol and was fully reassembled on stripped MR immune pellets. The whole MR-hsp90-based heterocomplex was transiently recovered in the soluble fraction of the nucleus after 10 min of incubation with aldosterone. Moreover, cross-linked MR-hsp90 heterocomplexes accumulated in the nucleus in a hormone-dependent manner, demonstrating that the heterocomplex can pass undissociated through the nuclear pore. On the other hand, a peptide that comprises the DNA-binding domain of MR impaired the nuclear export of MR, suggesting the involvement of this domain in the process. This study represents the first report describing the entire molecular system that commands MR nucleocytoplasmic trafficking and proposes that the MR-hsp90-TPR protein heterocomplex is dissociated in the nucleus rather than in the cytoplasm.

Indexed as

Active Transport, Cell NucleusAnimalsCell LineCell NucleusCHO CellsCricetinaeCricetulusDyneinsHSP90 Heat-Shock ProteinsHumansImmunophilinsMiceMicrotubulesMolecular Motor ProteinsMultiprotein ComplexesNIH 3T3 CellsDyneinsHSP90 Heat-Shock ProteinsImmunophilinsMolecular Motor ProteinsMultiprotein ComplexesNuclear Pore Complex ProteinsReceptors, MineralocorticoidRecombinant Proteinstacrolimus binding protein 4Tacrolimus Binding Proteins

Identifiers

PMID20038533
PMCPMC2820887
OpenAlexW2140949602

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.