Phosphorylation of the immunosuppressant FK506-binding protein FKBP52 by casein kinase II: Regulation of HSP90-binding activity of FKBP52

• DOI: 10.1073/pnas.94.26.14500
• Publication Date: 2002-07-26T14:42:40Z
• Authors: Yoshihiko Miyata; Béatrice Chambraud; Christine Radanyi; Jocelyne Leclerc; Marie-Claire Lebeau; Jack-Michel Renoir; Ryuichi Shirai; Maria-Grazia Catelli; Ichiro Yahara; Etienne-Emile Bau...
• Keywords: Casein kinase 2

FKBP52 (HSP56, p59, HBI) is the 59-kDa immunosuppressant FK506-binding protein and has peptidyl prolyl isomerase as well a chaperone-like activity in vitro . associates with heat shock HSP90 included steroid hormone receptor complexes vivo possesses conserved phosphorylation site for casein kinase II (CK2) that was previously shown to be associated HSP90. Here we examined whether phosphorylated by CK2 both Recombinant rabbit purified CK2. We expressed deletion mutants of determine site(s) Thr-143 hinge I region identified major A synthetic peptide corresponding this CK2, competitively inhibited other substrates The [ 32 P]phosphate labeling FKBP52-expressing cells revealed same also FK506 binding did not affect and, conversely, affected phosphorylation. Most importantly, CK2-phosphorylated bind These results indicate phosphorylates thus may regulate composition chaperone-containing such those receptors certain kinases.