Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β

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Glucocorticoid receptor (GR) is cytoplasmic in the absence of ligand and localizes to the nucleus after steroid binding. Previous evidence demonstrated that the hsp90-based heterocomplex bound to GR is required for the efficient retrotransport of the receptor to the nuclear compartment. We examined...

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Detalles Bibliográficos
Autores principales: Echeverría, P.C., Mazaira, G., Erlejman, A., Gomez-Sanchez, C., Pilipuk, G.P., Galigniana, M.D.
Formato: Artículo publishedVersion
Lenguaje:Inglés
Publicado: 2009
Materias:
digitonin
glucocorticoid receptor
glycoprotein
glycoprotein nup62
heat shock protein 70
heat shock protein 90
karyopherin beta
protein Fkbp52
protein p23
protein pp5
radicicol
steroid
tetratricopeptide repeat protein
unclassified drug
animal cell
article
cell membrane permeability
controlled study
human
human cell
mouse
nonhuman
nuclear import
nuclear pore
nuclear pore complex
priority journal
protein binding
protein cross linking
protein expression
protein function
protein protein interaction
structure analysis
tetratricopeptide repeat
Active Transport, Cell Nucleus
Animals
beta Karyopherins
Cell Line
Glycoproteins
HSP70 Heat-Shock Proteins
HSP90 Heat-Shock Proteins
Humans
Intramolecular Oxidoreductases
Mice
Multiprotein Complexes
Nuclear Pore
Nuclear Pore Complex Proteins
Receptors, Glucocorticoid
Tacrolimus Binding Proteins
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_02707306_v29_n17_p4788_Echeverria
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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