The majority of proteins must fold into their correct 3D structures in order to perform their biological functions. Under adverse conditions, proteins may become misfolded and accumulate into toxic aggregates. In order to maintain integrity of the proteome during stress, cells possess a vast network of chaperones and proteolytic systems which serve to counteract accumulation of misfolded proteins. This is mainly achieved via refolding, degradation or sequestration into non-toxic inclusions, and is an important mechanism to understand due to its association with neurodegenerative diseases and ageing.

My research aims to use a yeast model to understand the cellular responses to toxicity caused by protein misfolding and aggregation. A key focus will be to elucidate the role of the Ras/PKA pathway in mediating conditions which induce misfolding such as oxidative stress and heat shock.