The ability to preserve proteome integrity is essential for the long-term health of all cells. Numerous physiological and environmental conditions promote protein misfolding and damage, which can result in the appearance of protein aggregates. This is often referred to as a loss of protein homeostasis (proteostasis), and is highly detrimental. Therefore, cells have evolved a network of highly conserved protein quality control and stress response pathways that cooperate to prevent the appearance and persistence of misfolded and damaged proteins across the cell.
My lab uses the nematode worm C. elegans to understand how signals that promote growth, development, and reproduction early in life, influence proteostasis across tissues. Using a combination of molecular biology, genetics, and high-throughput methods, we study the impact of these pathways on ageing and disease susceptibility. Our ultimate goal is to identify new targets that can be manipulated pharmacologically to improve health.
Images of (left) polyglutamine(Q37)::YFP aggregation in C. elegans muscle cells and (right) polyglutamine(Q44)::YFP aggregation in C. elegans intestinal cells.