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

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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...

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Autores principales: Galigniana, M.D., Erlejman, A.G., Monte, M., Gomez-Sanchez, C., Piwien-Pilipuk, G.
Formato: Artículo publishedVersion
Lenguaje:Inglés
Publicado: 2010
Materias:
aldosterone
dynein adenosine triphosphatase
fk 506 binding protein
heat shock protein 90
immunophilin
mineralocorticoid receptor
molecular motor
protein fkbp52
tubulin
unclassified drug
animal cell
article
controlled study
human
human cell
mouse
nonhuman
priority journal
protein cross linking
protein domain
protein localization
protein protein interaction
tetratricopeptide repeat
Active Transport, Cell Nucleus
Animals
Cell Line
Cell Nucleus
CHO Cells
Cricetinae
Cricetulus
Dyneins
HSP90 Heat-Shock Proteins
Humans
Immunophilins
Mice
Microtubules
Molecular Motor Proteins
Multiprotein Complexes
NIH 3T3 Cells
Nuclear Pore
Nuclear Pore Complex Proteins
Protein Binding
Protein Stability
Protein Structure, Tertiary
Rats
Receptors, Mineralocorticoid
Recombinant Proteins
Tacrolimus Binding Proteins
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_02707306_v30_n5_p1285_Galigniana
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paperaa:paper_02707306_v30_n5_p1285_Galigniana
record_format dspace
spelling paperaa:paper_02707306_v30_n5_p1285_Galigniana2023-06-12T16:47:17Z The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events Mol. Cell. Biol. 2010;30(5):1285-1298 Galigniana, M.D. Erlejman, A.G. Monte, M. Gomez-Sanchez, C. Piwien-Pilipuk, G. aldosterone dynein adenosine triphosphatase fk 506 binding protein heat shock protein 90 immunophilin mineralocorticoid receptor molecular motor protein fkbp52 tubulin unclassified drug animal cell article controlled study human human cell mouse nonhuman priority journal protein cross linking protein domain protein localization protein protein interaction tetratricopeptide repeat Active Transport, Cell Nucleus Animals Cell Line Cell Nucleus CHO Cells Cricetinae Cricetulus Dyneins HSP90 Heat-Shock Proteins Humans Immunophilins Mice Microtubules Molecular Motor Proteins Multiprotein Complexes NIH 3T3 Cells Nuclear Pore Nuclear Pore Complex Proteins Protein Binding Protein Stability Protein Structure, Tertiary Rats Receptors, Mineralocorticoid Recombinant Proteins Tacrolimus Binding Proteins 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. Copyright © 2010, American Society for Microbiology. All Rights Reserved. Fil:Monte, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2010 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_02707306_v30_n5_p1285_Galigniana
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
language Inglés
orig_language_str_mv eng
topic aldosterone
dynein adenosine triphosphatase
fk 506 binding protein
heat shock protein 90
immunophilin
mineralocorticoid receptor
molecular motor
protein fkbp52
tubulin
unclassified drug
animal cell
article
controlled study
human
human cell
mouse
nonhuman
priority journal
protein cross linking
protein domain
protein localization
protein protein interaction
tetratricopeptide repeat
Active Transport, Cell Nucleus
Animals
Cell Line
Cell Nucleus
CHO Cells
Cricetinae
Cricetulus
Dyneins
HSP90 Heat-Shock Proteins
Humans
Immunophilins
Mice
Microtubules
Molecular Motor Proteins
Multiprotein Complexes
NIH 3T3 Cells
Nuclear Pore
Nuclear Pore Complex Proteins
Protein Binding
Protein Stability
Protein Structure, Tertiary
Rats
Receptors, Mineralocorticoid
Recombinant Proteins
Tacrolimus Binding Proteins
spellingShingle aldosterone
dynein adenosine triphosphatase
fk 506 binding protein
heat shock protein 90
immunophilin
mineralocorticoid receptor
molecular motor
protein fkbp52
tubulin
unclassified drug
animal cell
article
controlled study
human
human cell
mouse
nonhuman
priority journal
protein cross linking
protein domain
protein localization
protein protein interaction
tetratricopeptide repeat
Active Transport, Cell Nucleus
Animals
Cell Line
Cell Nucleus
CHO Cells
Cricetinae
Cricetulus
Dyneins
HSP90 Heat-Shock Proteins
Humans
Immunophilins
Mice
Microtubules
Molecular Motor Proteins
Multiprotein Complexes
NIH 3T3 Cells
Nuclear Pore
Nuclear Pore Complex Proteins
Protein Binding
Protein Stability
Protein Structure, Tertiary
Rats
Receptors, Mineralocorticoid
Recombinant Proteins
Tacrolimus Binding Proteins
Galigniana, M.D.
Erlejman, A.G.
Monte, M.
Gomez-Sanchez, C.
Piwien-Pilipuk, G.
The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events
topic_facet aldosterone
dynein adenosine triphosphatase
fk 506 binding protein
heat shock protein 90
immunophilin
mineralocorticoid receptor
molecular motor
protein fkbp52
tubulin
unclassified drug
animal cell
article
controlled study
human
human cell
mouse
nonhuman
priority journal
protein cross linking
protein domain
protein localization
protein protein interaction
tetratricopeptide repeat
Active Transport, Cell Nucleus
Animals
Cell Line
Cell Nucleus
CHO Cells
Cricetinae
Cricetulus
Dyneins
HSP90 Heat-Shock Proteins
Humans
Immunophilins
Mice
Microtubules
Molecular Motor Proteins
Multiprotein Complexes
NIH 3T3 Cells
Nuclear Pore
Nuclear Pore Complex Proteins
Protein Binding
Protein Stability
Protein Structure, Tertiary
Rats
Receptors, Mineralocorticoid
Recombinant Proteins
Tacrolimus Binding Proteins
description 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. Copyright © 2010, American Society for Microbiology. All Rights Reserved.
format Artículo
Artículo
publishedVersion
author Galigniana, M.D.
Erlejman, A.G.
Monte, M.
Gomez-Sanchez, C.
Piwien-Pilipuk, G.
author_facet Galigniana, M.D.
Erlejman, A.G.
Monte, M.
Gomez-Sanchez, C.
Piwien-Pilipuk, G.
author_sort Galigniana, M.D.
title The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events
title_short The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events
title_full The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events
title_fullStr The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events
title_full_unstemmed The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events
title_sort hsp90-fkbp52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events
publishDate 2010
url http://hdl.handle.net/20.500.12110/paper_02707306_v30_n5_p1285_Galigniana
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