Ph.D, University of Alberta
To maintain a healthy state, cells must constantly survey and regulate the quality of its proteins in a process called proteostasis. An integral component of the proteostasis system is a large group of proteins classified as molecular chaperones. Molecular chaperones recognize a myriad of misfolded substrates in cells and promote their proper folding or degradation via the formation of highly interconnected and adaptable networks consisting of other chaperones and the many facets of the proteostasis system.
The question of how molecular chaperones can effectively regulate the folding of hundreds of different proteins under a variety of challenging conditions including cellular stresses and disease states is of incredible interest to us. Moreover, we are dedicated to understanding how this robust molecular chaperone network ultimately fails in protein misfolding diseases such as Alzheimer’s Disease and Huntington’s Disease.
Our research is aimed at exposing the wiring of the molecular chaperone network in cells. We will use a blend of biochemical, cell biology and genetic approaches to profile and manipulate chaperone connections and functions. From this work, we hope to identify both the strengths and weaknesses in the molecular chaperone network and use these insights to better understand the cellular pathways that lead to disease.