TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stress

Autores
Gallo, Luciana Ines; Lagadari, Mariana; Piwien Pilipuk, Graciela; Galigniana, Mario Daniel
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Confocal microscopy images revealed that the tetratricopeptide repeat motif (TPR) domain immunophilin FKBP51 shows colocalization with the specific mitochondrial marker MitoTracker. Signal specificity was tested with different antibodies and by FKBP51 knockdown. This unexpected subcellular localization of FKBP51 was confirmed by colocalization studies with other mitochondrial proteins, biochemical fractionation, and electron microscopy imaging. Interestingly, FKBP51 forms complexes in mitochondria with the glucocorticoid receptor and the Hsp90/Hsp70-based chaperone heterocomplex. Although Hsp90 inhibitors favor FKBP51 translocation from mitochondria to the nucleus in a reversible manner, TPR domain-deficient mutants of FKBP51 are constitutively nuclear and fully excluded from mitochondria, suggesting that a functional TPR domain is required for its mitochondrial localization. FKBP51 overexpression protects cells against oxidative stress, whereas FKBP51 knockdown makes them more sensitive to injury. In summary, this is the first demonstration that FKBP51 is a major mitochondrial factor that undergoes nuclear-mitochondrial shuttling, an observation that may be related to antiapoptotic mechanisms triggered during the stress response.
Fil: Gallo, Luciana Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
Fil: Lagadari, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
Fil: Piwien Pilipuk, Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
Fil: Galigniana, Mario Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Materia
FKBP51
MITOCHONDRIA
APOPTOSIS
STRESS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/10887
Acceder
id CONICETDig_17ba084dabad68b80bdfb968961b344a
oai_identifier_str oai:ri.conicet.gov.ar:11336/10887
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stressGallo, Luciana InesLagadari, MarianaPiwien Pilipuk, GracielaGaligniana, Mario DanielFKBP51MITOCHONDRIAAPOPTOSISSTRESShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Confocal microscopy images revealed that the tetratricopeptide repeat motif (TPR) domain immunophilin FKBP51 shows colocalization with the specific mitochondrial marker MitoTracker. Signal specificity was tested with different antibodies and by FKBP51 knockdown. This unexpected subcellular localization of FKBP51 was confirmed by colocalization studies with other mitochondrial proteins, biochemical fractionation, and electron microscopy imaging. Interestingly, FKBP51 forms complexes in mitochondria with the glucocorticoid receptor and the Hsp90/Hsp70-based chaperone heterocomplex. Although Hsp90 inhibitors favor FKBP51 translocation from mitochondria to the nucleus in a reversible manner, TPR domain-deficient mutants of FKBP51 are constitutively nuclear and fully excluded from mitochondria, suggesting that a functional TPR domain is required for its mitochondrial localization. FKBP51 overexpression protects cells against oxidative stress, whereas FKBP51 knockdown makes them more sensitive to injury. In summary, this is the first demonstration that FKBP51 is a major mitochondrial factor that undergoes nuclear-mitochondrial shuttling, an observation that may be related to antiapoptotic mechanisms triggered during the stress response.Fil: Gallo, Luciana Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); ArgentinaFil: Lagadari, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); ArgentinaFil: Piwien Pilipuk, Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); ArgentinaFil: Galigniana, Mario Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaAmerican Society For Biochemistry And Molecular Biology2011-07-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/10887Gallo, Luciana Ines; Lagadari, Mariana; Piwien Pilipuk, Graciela; Galigniana, Mario Daniel; TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stress; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 286; 34; 5-7-2011; 30152-301600021-92581083-351Xenginfo:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/286/34/30152.longinfo:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M111.256610info:eu-repo/semantics/altIdentifier/url/www.ncbi.nlm.nih.gov/pmc/articles/PMC3191054info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:41:20Zoai:ri.conicet.gov.ar:11336/10887instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:41:20.434CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stress
title TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stress
spellingShingle TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stress
Gallo, Luciana Ines
FKBP51
MITOCHONDRIA
APOPTOSIS
STRESS
title_short TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stress
title_full TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stress
title_fullStr TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stress
title_full_unstemmed TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stress
title_sort TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stress
dc.creator.none.fl_str_mv Gallo, Luciana Ines
Lagadari, Mariana
Piwien Pilipuk, Graciela
Galigniana, Mario Daniel
author Gallo, Luciana Ines
author_facet Gallo, Luciana Ines
Lagadari, Mariana
Piwien Pilipuk, Graciela
Galigniana, Mario Daniel
author_role author
author2 Lagadari, Mariana
Piwien Pilipuk, Graciela
Galigniana, Mario Daniel
author2_role author
author
author
dc.subject.none.fl_str_mv FKBP51
MITOCHONDRIA
APOPTOSIS
STRESS
topic FKBP51
MITOCHONDRIA
APOPTOSIS
STRESS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Confocal microscopy images revealed that the tetratricopeptide repeat motif (TPR) domain immunophilin FKBP51 shows colocalization with the specific mitochondrial marker MitoTracker. Signal specificity was tested with different antibodies and by FKBP51 knockdown. This unexpected subcellular localization of FKBP51 was confirmed by colocalization studies with other mitochondrial proteins, biochemical fractionation, and electron microscopy imaging. Interestingly, FKBP51 forms complexes in mitochondria with the glucocorticoid receptor and the Hsp90/Hsp70-based chaperone heterocomplex. Although Hsp90 inhibitors favor FKBP51 translocation from mitochondria to the nucleus in a reversible manner, TPR domain-deficient mutants of FKBP51 are constitutively nuclear and fully excluded from mitochondria, suggesting that a functional TPR domain is required for its mitochondrial localization. FKBP51 overexpression protects cells against oxidative stress, whereas FKBP51 knockdown makes them more sensitive to injury. In summary, this is the first demonstration that FKBP51 is a major mitochondrial factor that undergoes nuclear-mitochondrial shuttling, an observation that may be related to antiapoptotic mechanisms triggered during the stress response.
Fil: Gallo, Luciana Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
Fil: Lagadari, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
Fil: Piwien Pilipuk, Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
Fil: Galigniana, Mario Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
description Confocal microscopy images revealed that the tetratricopeptide repeat motif (TPR) domain immunophilin FKBP51 shows colocalization with the specific mitochondrial marker MitoTracker. Signal specificity was tested with different antibodies and by FKBP51 knockdown. This unexpected subcellular localization of FKBP51 was confirmed by colocalization studies with other mitochondrial proteins, biochemical fractionation, and electron microscopy imaging. Interestingly, FKBP51 forms complexes in mitochondria with the glucocorticoid receptor and the Hsp90/Hsp70-based chaperone heterocomplex. Although Hsp90 inhibitors favor FKBP51 translocation from mitochondria to the nucleus in a reversible manner, TPR domain-deficient mutants of FKBP51 are constitutively nuclear and fully excluded from mitochondria, suggesting that a functional TPR domain is required for its mitochondrial localization. FKBP51 overexpression protects cells against oxidative stress, whereas FKBP51 knockdown makes them more sensitive to injury. In summary, this is the first demonstration that FKBP51 is a major mitochondrial factor that undergoes nuclear-mitochondrial shuttling, an observation that may be related to antiapoptotic mechanisms triggered during the stress response.
publishDate 2011
dc.date.none.fl_str_mv 2011-07-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/10887
Gallo, Luciana Ines; Lagadari, Mariana; Piwien Pilipuk, Graciela; Galigniana, Mario Daniel; TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stress; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 286; 34; 5-7-2011; 30152-30160
0021-9258
1083-351X
url http://hdl.handle.net/11336/10887
identifier_str_mv Gallo, Luciana Ines; Lagadari, Mariana; Piwien Pilipuk, Graciela; Galigniana, Mario Daniel; TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stress; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 286; 34; 5-7-2011; 30152-30160
0021-9258
1083-351X
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/286/34/30152.long
info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M111.256610
info:eu-repo/semantics/altIdentifier/url/www.ncbi.nlm.nih.gov/pmc/articles/PMC3191054
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society For Biochemistry And Molecular Biology
publisher.none.fl_str_mv American Society For Biochemistry And Molecular Biology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846083524563566592
score 13.22299

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