Client binding of Cdc37 is regulated intramolecularly and intermolecularly.
Recently we showed that the glycine-rich loop in the N-terminal portion of protein kinases and the client-binding site of Cdc37 are both necessary for interaction between Cdc37 and protein kinases. We demonstrate here that the N-terminal portion of Cdc37, distinct from its client-binding site, interacts with the C-terminal portion of Raf-1. This interaction might expose the client-binding site of Cdc37. In addition, we provide evidence indicating that Cdc37 is monomeric in its physiological state, and that it becomes a dimer only when it is complexed with both Hsp90 and protein kinases.
Terasawa
Kazuya
K
Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo.
Shinozaki
Fumika
F
Minami
Michiko
M
Minami
Yasufumi
Y
D000818:Animals; D019556:COS Cells; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D002522:Chlorocebus aethiops; D019281:Dimerization; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism; D011485:Protein Binding; D019908:Proto-Oncogene Proteins c-raf / Q000235:genetics / Q000378:metabolism
D018797:Cell Cycle Proteins; D018841:HSP90 Heat-Shock Proteins; D019908:Proto-Oncogene Proteins c-raf