Protein folding is required for the realization of genetic information at the level of functional proteins and as such is one of the most fundamental reactions in all of biology. A specialized class of proteins, so called molecular chaperones, is essential for the successful folding of many cellular proteins. The Department of Cellular Biochemistry at the Max Planck Institute of Biochemistry is investigating the mechanisms of protein folding in the cell, and studies how the machinery of molecular chaperones assists in co- and post-translational protein folding.
However even chaperones cannot prevent that a fraction of proteins misfold and aggregate. Such protein misfolding is increased in the presence of disease-associated mutations, external stress factors or as a result of aging. If proteins aggregate, organisms employ additional factors to either disaggregate and re-solubilize them, or transform them into aggregate species that are less dangerous to the cell. This machinery, together with the chaperone systems, is referred to as the proteostasis network, since it maintains protein homeostasis. Within the framework of ToPAG, we plan to analyze the relationship between protein aggregates and the proteostasis network, and search for ways to increase the ability of this network to handle the challenges of protein misfolding and aggregation.
More information: www.biochem.mpg.de/hartl