PD Dr. Matthias Mayer Regulation of protein conformation

Molecular chaperones of the Hsp70 and Hsp90 families are important players in de novo protein folding and refolding of stress-denatured and aggregated proteins. In addition, Hsp70 and Hsp90 proteins cooperatively interact with some 200 native proteins, so-called clients, regulating their activity and stability. Among these clients are many proteins involved in the control of cell homoeostasis, proliferation, differentiation and apoptosis. Not surprisingly, inhibitors of the chaperones are explored as potential therapeutica in pathological conditions, notably cancer and neurodegeneration. Our major research goal is to understand the mode of action of Hsp70 and Hsp90 chaperones and their influence on their clients. We therefore study their molecular mechanism, how Hsp70s bind native proteins, how these clients are transferred with the help of cochaperones onto Hsp90 and how these interactions influence the clients’ conformation and activity.

Detailed information on the project can be found at
www.zmbh.uni-heidelberg.de/Mayer/default.shtml