The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events

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In this study, we demonstrate that the subcellular localization of the mineralocorticoid receptor (MR) is regulated by tetratricopeptide domain (TPR) proteins. The high-molecular-weight immunophilin (IMM) FKBP52 links the MR-hsp90 complex to dynein/dynactin motors favoring the cytoplasmic transport...

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Detalles Bibliográficos
Autores principales: Galigniana, M.D., Erlejman, A.G., Monte, M., Gomez-Sanchez, C., Piwien-Pilipuk, G.
Formato: JOUR
Materias:
aldosterone
dynein adenosine triphosphatase
fk 506 binding protein
heat shock protein 90
immunophilin
mineralocorticoid receptor
molecular motor
protein fkbp52
tubulin
unclassified drug
animal cell
article
controlled study
human
human cell
mouse
nonhuman
priority journal
protein cross linking
protein domain
protein localization
protein protein interaction
tetratricopeptide repeat
Active Transport, Cell Nucleus
Animals
Cell Line
Cell Nucleus
CHO Cells
Cricetinae
Cricetulus
Dyneins
HSP90 Heat-Shock Proteins
Humans
Immunophilins
Mice
Microtubules
Molecular Motor Proteins
Multiprotein Complexes
NIH 3T3 Cells
Nuclear Pore
Nuclear Pore Complex Proteins
Protein Binding
Protein Stability
Protein Structure, Tertiary
Rats
Receptors, Mineralocorticoid
Recombinant Proteins
Tacrolimus Binding Proteins
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_02707306_v30_n5_p1285_Galigniana
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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