Biological actions of the hsp90-binding immunophilins FKBP51 and FKBP52

Immunophilins are a family of proteins whose signature domain is the peptidylprolyl-isomerase domain. High molecular weight immunophilins are characterized by the additional presence of tetratricopeptide-repeats (TPR) through which they bind to the 90-kDa heat-shock protein (Hsp90), and via this cha...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Zgajnar, N.R., De Leo, S.A., Lotufo, C.M., Erlejman, A.G., Pilipuk, G.P., Galigniana, M.D.
Formato: JOUR
Materias:
Cell differentiation
Dynein
FKBP51
FKBP52
Hsp90
Neurodifferentiation
NF-κB
Telomerase
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_2218273X_v9_n2_p_Zgajnar
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_2218273X_v9_n2_p_Zgajnar
record_format dspace
spelling todo:paper_2218273X_v9_n2_p_Zgajnar2023-10-03T16:40:42Z Biological actions of the hsp90-binding immunophilins FKBP51 and FKBP52 Zgajnar, N.R. De Leo, S.A. Lotufo, C.M. Erlejman, A.G. Pilipuk, G.P. Galigniana, M.D. Cell differentiation Dynein FKBP51 FKBP52 Hsp90 Neurodifferentiation NF-κB Telomerase Immunophilins are a family of proteins whose signature domain is the peptidylprolyl-isomerase domain. High molecular weight immunophilins are characterized by the additional presence of tetratricopeptide-repeats (TPR) through which they bind to the 90-kDa heat-shock protein (Hsp90), and via this chaperone, immunophilins contribute to the regulation of the biological functions of several client-proteins. Among these Hsp90-binding immunophilins, there are two highly homologous members named FKBP51 and FKBP52 (FK506-binding protein of 51-kDa and 52-kDa, respectively) that were first characterized as components of the Hsp90-based heterocomplex associated to steroid receptors. Afterwards, they emerged as likely contributors to a variety of other hormone-dependent diseases, stress-related pathologies, psychiatric disorders, cancer, and other syndromes characterized by misfolded proteins. The differential biological actions of these immunophilins have been assigned to the structurally similar, but functionally divergent enzymatic domain. Nonetheless, they also require the complementary input of the TPR domain, most likely due to their dependence with the association to Hsp90 as a functional unit. FKBP51 and FKBP52 regulate a variety of biological processes such as steroid receptor action, transcriptional activity, protein conformation, protein trafficking, cell differentiation, apoptosis, cancer progression, telomerase activity, cytoskeleton architecture, etc. In this article we discuss the biology of these events and some mechanistic aspects. © 2019 by the authors. Licensee MDPI, Basel, Switzerland. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_2218273X_v9_n2_p_Zgajnar
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Cell differentiation
Dynein
FKBP51
FKBP52
Hsp90
Neurodifferentiation
NF-κB
Telomerase
spellingShingle Cell differentiation
Dynein
FKBP51
FKBP52
Hsp90
Neurodifferentiation
NF-κB
Telomerase
Zgajnar, N.R.
De Leo, S.A.
Lotufo, C.M.
Erlejman, A.G.
Pilipuk, G.P.
Galigniana, M.D.
Biological actions of the hsp90-binding immunophilins FKBP51 and FKBP52
topic_facet Cell differentiation
Dynein
FKBP51
FKBP52
Hsp90
Neurodifferentiation
NF-κB
Telomerase
description Immunophilins are a family of proteins whose signature domain is the peptidylprolyl-isomerase domain. High molecular weight immunophilins are characterized by the additional presence of tetratricopeptide-repeats (TPR) through which they bind to the 90-kDa heat-shock protein (Hsp90), and via this chaperone, immunophilins contribute to the regulation of the biological functions of several client-proteins. Among these Hsp90-binding immunophilins, there are two highly homologous members named FKBP51 and FKBP52 (FK506-binding protein of 51-kDa and 52-kDa, respectively) that were first characterized as components of the Hsp90-based heterocomplex associated to steroid receptors. Afterwards, they emerged as likely contributors to a variety of other hormone-dependent diseases, stress-related pathologies, psychiatric disorders, cancer, and other syndromes characterized by misfolded proteins. The differential biological actions of these immunophilins have been assigned to the structurally similar, but functionally divergent enzymatic domain. Nonetheless, they also require the complementary input of the TPR domain, most likely due to their dependence with the association to Hsp90 as a functional unit. FKBP51 and FKBP52 regulate a variety of biological processes such as steroid receptor action, transcriptional activity, protein conformation, protein trafficking, cell differentiation, apoptosis, cancer progression, telomerase activity, cytoskeleton architecture, etc. In this article we discuss the biology of these events and some mechanistic aspects. © 2019 by the authors. Licensee MDPI, Basel, Switzerland.
format JOUR
author Zgajnar, N.R.
De Leo, S.A.
Lotufo, C.M.
Erlejman, A.G.
Pilipuk, G.P.
Galigniana, M.D.
author_facet Zgajnar, N.R.
De Leo, S.A.
Lotufo, C.M.
Erlejman, A.G.
Pilipuk, G.P.
Galigniana, M.D.
author_sort Zgajnar, N.R.
title Biological actions of the hsp90-binding immunophilins FKBP51 and FKBP52
title_short Biological actions of the hsp90-binding immunophilins FKBP51 and FKBP52
title_full Biological actions of the hsp90-binding immunophilins FKBP51 and FKBP52
title_fullStr Biological actions of the hsp90-binding immunophilins FKBP51 and FKBP52
title_full_unstemmed Biological actions of the hsp90-binding immunophilins FKBP51 and FKBP52
title_sort biological actions of the hsp90-binding immunophilins fkbp51 and fkbp52
url http://hdl.handle.net/20.500.12110/paper_2218273X_v9_n2_p_Zgajnar
work_keys_str_mv AT zgajnarnr biologicalactionsofthehsp90bindingimmunophilinsfkbp51andfkbp52
AT deleosa biologicalactionsofthehsp90bindingimmunophilinsfkbp51andfkbp52
AT lotufocm biologicalactionsofthehsp90bindingimmunophilinsfkbp51andfkbp52
AT erlejmanag biologicalactionsofthehsp90bindingimmunophilinsfkbp51andfkbp52
AT pilipukgp biologicalactionsofthehsp90bindingimmunophilinsfkbp51andfkbp52
AT galignianamd biologicalactionsofthehsp90bindingimmunophilinsfkbp51andfkbp52
_version_ 1807314797089259520

Ejemplares similares