Evidence map›Paper›PMID 27233944›Full record

ArticleMolecular oncology2016

Hsp90-binding immunophilin FKBP51 forms complexes with hTERT enhancing telomerase activity.

Mariana Lagadari, Nadia R Zgajnar, Luciana I Gallo, Mario D Galigniana

RetractedOpen access · bronzeAbstract readRetracted Publication
In one paragraph

Article in Molecular oncology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-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

20 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
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  9. Review
  10. Heat Shock Protein 90 as Therapeutic Target for CVDs and Heart Ageing.International journal of molecular sciences · 2022
    Review
  11. The Connection Between Cell Fate and Telomere.Advances in experimental medicine and biology · 2021
    Review
  12. Review
  13. Article
  14. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 2 countries.

Mariana LagadariInstituto de Biología y Medicina Experimental (IBYME)-CONICET, Buenos Aires, C1428ADN, Argentina.
Nadia R ZgajnarInstituto de Biología y Medicina Experimental (IBYME)-CONICET, Buenos Aires, C1428ADN, Argentina.
Luciana I GalloInstituto de Fisiología, Biología Molecular y Neurociencias (CONICET) & Departamento de Fisiología, Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, C1428EGA, Argentina.
Mario D GalignianaInstituto de Biología y Medicina Experimental (IBYME)-CONICET, Buenos Aires, C1428ADN, Argentina; Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, C1428EGA, Argentina. Electronic address: mgaligniana@conicet.gov.ar.
Consejo Nacional de Investigaciones Científicas y Técnicas · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FK506-binding proteins are members of the immunophilin family of proteins. Those immunophilins associated to the 90-kDa-heat-shock protein, Hsp90, have been proposed as potential modulators of signalling cascade factors chaperoned by Hsp90. FKBP51 and FKBP52 are the best characterized Hsp90-bound immunophilins first described associated to steroid-receptors. The reverse transcriptase subunit of telomerase, hTERT, is also an Hsp90 client-protein and is highly expressed in cancer cells, where it is required to compensate the loss of telomeric DNA after each successive cell division. Because FKBP51 is also a highly expressed protein in cancer tissues, we analyzed its potential association with hTERT·Hsp90 complexes and its possible biological role. In this study it is demonstrated that both immunophilins, FKBP51 and FKBP52, co-immunoprecipitate with hTERT. The Hsp90 inhibitor radicicol disrupts the heterocomplex and favors the partial cytoplasmic relocalization of hTERT in similar manner as the overexpression of the TPR-domain peptide of the immunophilin. While confocal microscopy images show that FKBP51 is primarily localized in mitochondria and hTERT is totally nuclear, upon the onset of oxidative stress, FKBP51 (but not FKBP52) becomes mostly nuclear colocalizing with hTERT, and longer exposure times to peroxide favors hTERT export to mitochondria. Importantly, telomerase activity of hTERT is significantly enhanced by FKBP51. These observations support the emerging role assigned to FKBP51 as antiapoptotic factor in cancer development and progression, and describe for the first time the potential role of this immunophilin favoring the clonal expansion by enhancing telomerase activity.

Indexed as

Cell Line, TumorCell NucleusCell SurvivalHSP90 Heat-Shock ProteinsHumansMitochondriaOxidative StressProteasome Endopeptidase ComplexProtein BindingProteolysisTacrolimus Binding Protein 5Tacrolimus Binding ProteinsTelomeraseHSP90 Heat-Shock ProteinsProteasome Endopeptidase ComplexTacrolimus Binding Protein 5Tacrolimus Binding ProteinsTelomeraseFKBP51FKBP52Hsp90hTERTImmunophilinTelomerase

Identifiers

PMID27233944
PMCPMC5423183
OpenAlexW2403642978

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.