Fig. 2
From: Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
![Fig. 2](http://media.springernature.com/full/springer-static/image/art%3A10.1186%2Fs13045-018-0602-8/MediaObjects/13045_2018_602_Fig2_HTML.gif)
A speculative model for the Hsp90-Cdc37-client protein cycle. Cdc37 first tests the proper substrates and establishes stable connection with the client protein to create a Cdc37-client protein binary complex. Then, the binary complex binds to Hsp90 to form a ternary complex. The formation of the Hsp90-Cdc37-client protein ternary complex finally facilitates client protein loading onto the Hsp90 chaperone machinery. It is worthy of note that Cdc37 will be phosphorylated by casein kinase 2 (CK2) at Ser13 before connecting with client proteins and dephosphorylated by the protein phosphatase 5 (PP5) before client protein release