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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Detalles Bibliográficos
Publicado: 2015
Materias:
P50
P65
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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spelling 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