Regulation of NF-κB signalling cascade by immunophilins
The fine regulation of signalling cascades is a key event required to maintain the appropriate functional properties of a cell when a given stimulus triggers specific biological responses. In this sense, cumulative experimental evidence during the last years has shown that high molecular weight immu...
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_18744672_v9_n2_p99_Lagadari http://hdl.handle.net/20.500.12110/paper_18744672_v9_n2_p99_Lagadari |
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paper:paper_18744672_v9_n2_p99_Lagadari2023-06-08T16:30:06Z Regulation of NF-κB signalling cascade by immunophilins FK506 FKBP51 FKBP52 Hsp70 Hsp90 NF-κB P50 P65 chaperone FK506 binding protein 51 FK506 binding protein 52 heat shock protein 90 I kappa B immunophilin steroid receptor unclassified drug fk 506 binding protein heat shock protein 90 immunoglobulin enhancer binding protein tacrolimus binding protein 4 tacrolimus binding protein 5 Article cells by body anatomy DNA determination DNA sequence DNA structure in vitro study inflammation innate immunity ligand binding lipid metabolism molecular weight nonhuman priority journal promoter region protein analysis protein binding protein degradation protein expression protein function protein interaction protein phosphorylation signal transduction animal chemistry human metabolism protein conformation Animals HSP90 Heat-Shock Proteins Humans NF-kappa B Protein Conformation Signal Transduction Tacrolimus Binding Proteins The fine regulation of signalling cascades is a key event required to maintain the appropriate functional properties of a cell when a given stimulus triggers specific biological responses. In this sense, cumulative experimental evidence during the last years has shown that high molecular weight immunophilins possess a fundamental importance in the regulation of many of these processes. It was first discovered that TPR-domain immunophilins such as FKBP51 and FKBP52 play a cardinal role, usually in an antagonistic fashion, in the regulation of several members of the steroid receptor family via its interaction with the heat-shock protein of 90-kDa, Hsp90. These Hsp90-associated cochaperones form a functional unit with the molecular chaperone influencing ligand binding capacity, receptor trafficking, and hormone-dependent transcriptional activity. Recently, it was demonstrated that the same immunophilins are also able to regulate the NF-κB signalling cascade in an Hsp90 independent manner. In this article we analize these properties and discuss the relevance of this novel regulatory pathway in the context of the pleiotropic actions managed by NF-κB in several cell types and tissues. © 2016 Bentham Science Publishers. 2015 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_18744672_v9_n2_p99_Lagadari http://hdl.handle.net/20.500.12110/paper_18744672_v9_n2_p99_Lagadari |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
FK506 FKBP51 FKBP52 Hsp70 Hsp90 NF-κB P50 P65 chaperone FK506 binding protein 51 FK506 binding protein 52 heat shock protein 90 I kappa B immunophilin steroid receptor unclassified drug fk 506 binding protein heat shock protein 90 immunoglobulin enhancer binding protein tacrolimus binding protein 4 tacrolimus binding protein 5 Article cells by body anatomy DNA determination DNA sequence DNA structure in vitro study inflammation innate immunity ligand binding lipid metabolism molecular weight nonhuman priority journal promoter region protein analysis protein binding protein degradation protein expression protein function protein interaction protein phosphorylation signal transduction animal chemistry human metabolism protein conformation Animals HSP90 Heat-Shock Proteins Humans NF-kappa B Protein Conformation Signal Transduction Tacrolimus Binding Proteins |
spellingShingle |
FK506 FKBP51 FKBP52 Hsp70 Hsp90 NF-κB P50 P65 chaperone FK506 binding protein 51 FK506 binding protein 52 heat shock protein 90 I kappa B immunophilin steroid receptor unclassified drug fk 506 binding protein heat shock protein 90 immunoglobulin enhancer binding protein tacrolimus binding protein 4 tacrolimus binding protein 5 Article cells by body anatomy DNA determination DNA sequence DNA structure in vitro study inflammation innate immunity ligand binding lipid metabolism molecular weight nonhuman priority journal promoter region protein analysis protein binding protein degradation protein expression protein function protein interaction protein phosphorylation signal transduction animal chemistry human metabolism protein conformation Animals HSP90 Heat-Shock Proteins Humans NF-kappa B Protein Conformation Signal Transduction Tacrolimus Binding Proteins Regulation of NF-κB signalling cascade by immunophilins |
topic_facet |
FK506 FKBP51 FKBP52 Hsp70 Hsp90 NF-κB P50 P65 chaperone FK506 binding protein 51 FK506 binding protein 52 heat shock protein 90 I kappa B immunophilin steroid receptor unclassified drug fk 506 binding protein heat shock protein 90 immunoglobulin enhancer binding protein tacrolimus binding protein 4 tacrolimus binding protein 5 Article cells by body anatomy DNA determination DNA sequence DNA structure in vitro study inflammation innate immunity ligand binding lipid metabolism molecular weight nonhuman priority journal promoter region protein analysis protein binding protein degradation protein expression protein function protein interaction protein phosphorylation signal transduction animal chemistry human metabolism protein conformation Animals HSP90 Heat-Shock Proteins Humans NF-kappa B Protein Conformation Signal Transduction Tacrolimus Binding Proteins |
description |
The fine regulation of signalling cascades is a key event required to maintain the appropriate functional properties of a cell when a given stimulus triggers specific biological responses. In this sense, cumulative experimental evidence during the last years has shown that high molecular weight immunophilins possess a fundamental importance in the regulation of many of these processes. It was first discovered that TPR-domain immunophilins such as FKBP51 and FKBP52 play a cardinal role, usually in an antagonistic fashion, in the regulation of several members of the steroid receptor family via its interaction with the heat-shock protein of 90-kDa, Hsp90. These Hsp90-associated cochaperones form a functional unit with the molecular chaperone influencing ligand binding capacity, receptor trafficking, and hormone-dependent transcriptional activity. Recently, it was demonstrated that the same immunophilins are also able to regulate the NF-κB signalling cascade in an Hsp90 independent manner. In this article we analize these properties and discuss the relevance of this novel regulatory pathway in the context of the pleiotropic actions managed by NF-κB in several cell types and tissues. © 2016 Bentham Science Publishers. |
title |
Regulation of NF-κB signalling cascade by immunophilins |
title_short |
Regulation of NF-κB signalling cascade by immunophilins |
title_full |
Regulation of NF-κB signalling cascade by immunophilins |
title_fullStr |
Regulation of NF-κB signalling cascade by immunophilins |
title_full_unstemmed |
Regulation of NF-κB signalling cascade by immunophilins |
title_sort |
regulation of nf-κb signalling cascade by immunophilins |
publishDate |
2015 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_18744672_v9_n2_p99_Lagadari http://hdl.handle.net/20.500.12110/paper_18744672_v9_n2_p99_Lagadari |
_version_ |
1768543966524866560 |