Dr Christine Salaun

Personal statement

Over the last ten years, S-acylation has emerged as a prominent protein post-translational modification that impacts all physiological systems and is associated with many different disease states, including cancer, neurological disorders and diabetes. Quantitative proteomics approaches have indicated that up to 10% of the proteome is modified by S-acylation, and this can affect protein localisation, stability, interactions and function. A family of twenty-three DHHC acyltransferase enzymes whose mechanism of action and regulation are poorly understood mediates S-acylation. Since joining Prof Chamberlain’s group at the University of Strathclyde in 2012, I have been involved in various projects exploring the regulation of DHHC cellular localization in neurons (in collaboration with Dr Trevor Bushell), and in the mechanisms underlying DHHC enzyme-substrate recognition and specificity. S-acylation has received growing interest from Pharma as a potential novel therapeutic target for a range of diseases. However, we lack selective inhibitors of the DHHC enzyme family. I was involved in a collaborative project (with Prof Nicholas Tomkinson) and the Japanese company Ono Pharma Ltd that led to the discovery of novel inhibitors of DHHC enzymes.

I am currently developing projects exploring the contribution of S-acylation to viral biology.