The Hsp90-Hsp70 chaperone system
Key players of the folding machinery in the eukaryotic cytosol are the ATP-dependent Hsp90 and Hsp70 chaperones and their co-chaperones. For many proteins, the two machineries work together and are even physically linked by specific proteins. Hsp70 and Hsp90 can be seen as basic modules to which additional functions or modes can be attached via co-chaperones. This allows the conformational processing of client proteins which are dependent on the help of chaperones. These include key regulator of many cellular processes such as steroid hormone receptors, kinases, transcription factors and many more. Our work focuses on defining their mode of action, specifically the chaperone client interaction and the transfer of clients between chaperone systems by combining in vitro and in vivo approaches.