Corticosteroid receptors as a model for the Hsp90•immunophilin-based transport machinery.
corticosteroid receptor
dynein
heat-shock protein
immunophilin, TPR domain
molecular chaperone
Journal
Trends in endocrinology and metabolism: TEM
ISSN: 1879-3061
Titre abrégé: Trends Endocrinol Metab
Pays: United States
ID NLM: 9001516
Informations de publication
Date de publication:
10 2021
10 2021
Historique:
received:
31
05
2021
revised:
23
07
2021
accepted:
26
07
2021
pubmed:
24
8
2021
medline:
9
2
2022
entrez:
23
8
2021
Statut:
ppublish
Résumé
Steroid receptors form soluble heterocomplexes with the 90-kDa heat-shock protein (Hsp90) and other chaperones and co-chaperones. The assembly and composition of the oligomer is influenced by the presence and nature of the bound steroid. Although these receptors shuttle dynamically in and out of the nucleus, their primary localization in the absence of steroid can be mainly cytoplasmic, mainly nuclear, or partitioned into both cellular compartments. Upon steroid binding, receptors become localized to the nucleus via the transportosome, a retrotransport molecular machinery that comprises Hsp90, a high-molecular-weight immunophilin, and dynein motors. This molecular machinery, first evidenced in steroid receptors, can also be used by other soluble proteins. In this review, we dissect the complete model of this transport machinery system.
Identifiants
pubmed: 34420854
pii: S1043-2760(21)00171-5
doi: 10.1016/j.tem.2021.07.005
pii:
doi:
Substances chimiques
HSP90 Heat-Shock Proteins
0
Molecular Chaperones
0
Receptors, Glucocorticoid
0
Receptors, Steroid
0
Immunophilins
EC 5.2.1.8
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
827-838Informations de copyright
Copyright © 2021 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests None declared by authors.