Christian Schlieker PhD
Assistant Professor of Molecular Biophysics and Biochemistry
Protein folding; ubiquitin; Protein quality control and its relation to viral pathogenesis
Defects in protein folding have been identified as an underlying cause for a steadily increasing number of congenital diseases, yet the connection between protein misfolding and disease remains poorly understood. My lab studies how a cell decides whether a misfolded protein is repaired or must be degraded, and how this process is controlled at the molecular level. In higher eukaryotes, the ubiquitin / proteasome system and the lysosome cooperate to dispose of defective proteins. We apply a combination of structural, biochemical, and cell biological approaches to dissect the multiple roles of ubiquitin in protein quality control. One of our immediate goals is to decipher the largely enigmatic role of deubiquitinating enzymes, which counterbalance the activity of ubiquitin ligases. Our long-term goal is to understand why and how misfolded proteins are partitioned between cellular compartments and to dissect how individual branches of the protein quality control network are wired to form a robust network.