Prof. Thorsten Hoppe and his team are using the nematode Caenorhabditis elegans to study physiological aspects of selective protein turnover in the context of aging-associated processes, such as muscle development and regeneration, protein aggregation, and genome stability. They take advantage of fluorescent reporter proteins that allow them to evaluate the activity of both 26S proteasome and autophagy in transgenic worms. This approach has already been used for genetic screening, which provides insight into the regulation of the proteolytic machinery. Initial results indicate that the dynamics of different proteolytic pathways are controlled by stress-induced signaling mechanisms. Identifying the critical regulators would help to characterize the underlying principles. In addition to intracellular proteostasis networks, Hoppe and his team’s long-term mission is to understand non-cell-autonomous regulation of protein degradation through paracrine factors. Intercellular communication via stress signals may coordinate cells of different tissues and counteract the aging process of the organism as a whole. The team’s goal is to understand the crosstalk between stress-induced proteolytic pathways and the aging of multicellular organisms.