The ensemble of molecular chaperones are central components of the cellular machinery that establishes and maintains protein homeostasis. Chaperones assist native folding of newly synthesized proteins and repair and eliminate misfolded and aggregated proteins, and therefore have fundamental impact on cell physiology, aging and disease. The goal of our research is to understand the intricate functional network of chaperones and its interplay with proteases in protein biogenesis and quality control, and the molecular working principles of chaperone machines. Furthermore, we want to elucidate causes and consequences of protein aggregation related to disease, in particular neurodegeneration and cancer. As models we are using E. coli, S. cerevisiae, C. elegans and human cells, and we are employing multi-disciplinary approaches ranging from genetics and molecular biology to biochemistry and biophysics. Currently we have three main research themes:
1. Mechanisms of folding and assembly of newly synthesized proteins.
2. Mechanisms of protein quality control.
3. Propagation of protein misfolding in neurodegenerative diseases (Project group Carmen Nussbaum-Krammer).