Fatty acylation, the covalent attachment of long chain fatty acids to proteins, is a critical cellular control mechanism. Indeed, fatty acylation impacts on virtually every aspect of cellular life. Fatty acylated proteins are surprisingly abundant and form an understudied group of proteins. The two main types of fatty acylation are myristoylation and palmitoylation. Many fatty acylated proteins are linked to the disease state. Examples include: Src, Ras and Wnt oncogenic proteins are involved in cancer progression while viral acylated HIV Gag and GP160 are involved in the HIV life cycle and AIDS. In addition, G-protein coupled receptors are involved in a variety of patho-physiological conditions such as hypertension (e.g. β-adrenergic and vasopressin receptors). Studying fatty acylation is therefore highly clinically relevant. We have focused on cancer and cardiovascular diseases as our pathophysiological models. Together, these account for 60% of all deaths in Canada. Thus, studying protein fatty acylation in the context of cancer and cardiovascular is invaluable to human health. More specifically, my laboratory studies the role of protein fatty acylation across the full spectrum of signal transduction. Simply put, signal transduction is the movement of a signal from outside to inside the cell. It often results in changes in gene expression, which in turn, alters cellular metabolism. In one project, we study the role of protein fatty acylation in membrane localization as it pertains to cancer. In a second project project, we study the involvement of palmitoylation in the regulation of gene expression and enzymatic activity resulting in the fine-tuning of mitochondrial metabolism. More information can be found on our University of Alberta website:http://www.cellbiology.ualberta.ca/en/FacultyMembers/LucBerthiaume

Chief Scientific Officer and Co-founder at Pacylex Pharmaceuticals, Inc.Original CEO from August 2012-December 2017