Inhibition of GR‐mediated transcription by p23 requires interaction with Hsp90

FEBS Letters

Holsboer, Florian¹  Hartl, F.Ulrich²  Rein, Theo¹  Schmidt, Ulrike¹  Young, Jason C.²  Wochnik, Gabriela M.¹ 

[1] Max Planck Institute of Psychiatry, Kraepelinstraße 10, D-80804 Munich, Germany;Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany

关键词: Glucocorticoid receptor;    Heat shock protein 90;    p23;    Chaperone;    Co-chaperone;    GFP;    green fluorescence protein;    GR;    glucocorticoid receptor;    Hsp;    heat shock protein;   

DOI  :  10.1016/S0014-5793(04)00066-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown