Functions of the Hsp90-binding FKBP immunophilins

Hsp90 functionally interacts with a broad array of client proteins, but in every case examined Hsp90 is accompanied by one or more co-chaperones. One class of co-chaperone contains a tetratricopeptide repeat domain that targets the co-chaperone to the C-terminal region of Hsp90. Within this class ar...

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Guardado en:
Detalles Bibliográficos
Publicado: 2015
Materias:
FKBP
Hsp90
Immunophilin
Steroid hormone receptor
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03060225_v78_n_p1_Guy
http://hdl.handle.net/20.500.12110/paper_03060225_v78_n_p1_Guy
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_03060225_v78_n_p1_Guy
record_format dspace
spelling paper:paper_03060225_v78_n_p1_Guy2023-06-08T15:31:03Z Functions of the Hsp90-binding FKBP immunophilins FKBP Hsp90 Immunophilin Steroid hormone receptor Hsp90 functionally interacts with a broad array of client proteins, but in every case examined Hsp90 is accompanied by one or more co-chaperones. One class of co-chaperone contains a tetratricopeptide repeat domain that targets the co-chaperone to the C-terminal region of Hsp90. Within this class are Hsp90-binding peptidylprolyl isomerases, most of which belong to the FK506-binding protein (FKBP) family. Despite the common association of FKBP co-chaperones with Hsp90, it is now clear that the client protein influences, and is influenced by, the particular FKBP bound to Hsp90. Examples include Xap2 in aryl hydrocarbon receptor complexes and FKBP52 in steroid receptor complexes. In this chapter, we discuss the known functional roles played by FKBP co-chaperones and, where possible, relate distinctive functions to structural differences between FKBP members. © Springer International Publishing Switzerland 2015 2015 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03060225_v78_n_p1_Guy http://hdl.handle.net/20.500.12110/paper_03060225_v78_n_p1_Guy
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic FKBP
Hsp90
Immunophilin
Steroid hormone receptor
spellingShingle FKBP
Hsp90
Immunophilin
Steroid hormone receptor
Functions of the Hsp90-binding FKBP immunophilins
topic_facet FKBP
Hsp90
Immunophilin
Steroid hormone receptor
description Hsp90 functionally interacts with a broad array of client proteins, but in every case examined Hsp90 is accompanied by one or more co-chaperones. One class of co-chaperone contains a tetratricopeptide repeat domain that targets the co-chaperone to the C-terminal region of Hsp90. Within this class are Hsp90-binding peptidylprolyl isomerases, most of which belong to the FK506-binding protein (FKBP) family. Despite the common association of FKBP co-chaperones with Hsp90, it is now clear that the client protein influences, and is influenced by, the particular FKBP bound to Hsp90. Examples include Xap2 in aryl hydrocarbon receptor complexes and FKBP52 in steroid receptor complexes. In this chapter, we discuss the known functional roles played by FKBP co-chaperones and, where possible, relate distinctive functions to structural differences between FKBP members. © Springer International Publishing Switzerland 2015
title Functions of the Hsp90-binding FKBP immunophilins
title_short Functions of the Hsp90-binding FKBP immunophilins
title_full Functions of the Hsp90-binding FKBP immunophilins
title_fullStr Functions of the Hsp90-binding FKBP immunophilins
title_full_unstemmed Functions of the Hsp90-binding FKBP immunophilins
title_sort functions of the hsp90-binding fkbp immunophilins
publishDate 2015
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03060225_v78_n_p1_Guy
http://hdl.handle.net/20.500.12110/paper_03060225_v78_n_p1_Guy
_version_ 1768543946240163840

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