Inhibition of GR-mediated transcription by p23 requires interaction with Hsp90.
p23 is a regulatory co-chaperone of heat shock protein (Hsp) 90, but can also act as a general molecular chaperone by itself. Using novel point mutations of p23 that disrupt its interaction with Hsp90 we found its co-chaperone function to be required for its inhibitory effect on glucocorticoid receptor (GR). ... The C-terminal region of p23, which is required for its chaperone activity, is dispensable for inhibition of GR. Importantly, similar results were obtained with a constitutively active GR. Thus, the action of p23 on the nuclear stage of GR regulation requires its Hsp90 co-chaperone function, but not its chaperone activity.
Mesh Terms:
Amino Acid Substitution, Cell Line, Tumor, Cell Nucleus, Clone Cells, DNA-Binding Proteins, Green Fluorescent Proteins, HSP90 Heat-Shock Proteins, HeLa Cells, Humans, Luciferases, Luminescent Proteins, Neuroblastoma, Point Mutation, Precipitin Tests, Protein Structure, Tertiary, Receptors, Glucocorticoid, Recombinant Proteins, Structure-Activity Relationship, Transcription, Genetic, Transfection
Amino Acid Substitution, Cell Line, Tumor, Cell Nucleus, Clone Cells, DNA-Binding Proteins, Green Fluorescent Proteins, HSP90 Heat-Shock Proteins, HeLa Cells, Humans, Luciferases, Luminescent Proteins, Neuroblastoma, Point Mutation, Precipitin Tests, Protein Structure, Tertiary, Receptors, Glucocorticoid, Recombinant Proteins, Structure-Activity Relationship, Transcription, Genetic, Transfection
FEBS Lett.
Date: Feb. 27, 2004
PubMed ID: 14987994
View in: Pubmed Google Scholar
Download Curated Data For This Publication
187613
Switch View:
- Interactions 2