Gassaway Lab

With the advent of mass spectrometry based proteomics and improved phosphopeptide enrichment, it is now feasible to detect thousands of phosphorylation events in a given experiment. However, the functional role for >94% of these events is completely unknown and those that do have some functional annotation are often inaccurate or incomplete despite the ubiquity and importance of this post-translational modification. I am dedicated to developing tools and methods to bridge this gap between phosphorylation site detection and functional understanding. To this end, proteome thermal stability methods, including the Proteome Integrated Thermal Shift Assay (PITSA) that I developed, have the potential to identify phosphorylation sites or other protein post-translational modifications with altered biophysical states, which are presumably correlated with functional changes in the protein. Additionally, phospho-amino acid orthogonal translation systems offer powerful tools to generate and study phosphorylated proteins. Using these techniques, my lab will characterize the role(s) of protein phosphorylation and other post-translational modifications in a variety of contexts, including cancer, neurodegeneration, and aging.