Project Team: Scott Napper, Philip Griebel, Erin Scruten
Phosphorylation is the predominant mechanism of post-translational modification for regulation of protein function. With central roles in virtually every cellular process, and strong linkages with many diseases, there is a considerable interest in defining and ultimately controlling kinase activities. Kinases are attractive targets for drug design, with kinase inhibitors a primary area of drug development for many diseases, including infections.
Investigations of human cellular phosphorylation events, which include over 500 different kinases and tens of thousands of phosphorylation targets, are a daunting challenge for proteomic researchers and cell biologists. As such, tools are needed that enable the evaluation of cellular phosphorylation events in a high-throughput, and biologically relevant fashion. Towards this objective, methodologies for the creation of species-specific peptide arrays, and a software platform for analysis of kinomic data have been developed. These tools have been applied to a numerous species to investigate pathophysiological states such as a number of infection models, inflammation, cancer and biomarker discovery.