Brandon Gassaway is an Assistant Professor in the Department of Chemistry & Biochemistry at Brigham Young University, whose research focuses on functionalizing protein post-translational modifications using thermal stability proteomics and phospho-amino acid orthogonal translation systems. Brandon graduated Magna Cum Laude with university honors from Brigham Young University, where he worked in the laboratory of Dr. Emily Bates studying the role of inwardly-rectifying potassium channels in Drosophila development. As a part of this research, Brandon was awarded a NSF Graduate Research Fellowship.
Brandon went on to do his graduate studies with Dr. Jesse Rinehart at Yale University, where he investigated mechanisms of insulin resistance using phosphoproteomic analysis. While at Yale, Brandon was named to the inaugural class of Gruber Fellows, as well as completed the Medical Research Scholars Program and received the Certificate of College Teaching Preparation. Brandon then began a post-doctoral fellowship in the laboratory of Dr. Steven Gygi, where he developed methods to functionalize protein post-translational modifications. During his fellowship, Brandon also joined the laboratory of Dr. Marcia Haigis, where he applied the methods he developed in the Gygi lab to models of T cell activation, as well as various cancer models.
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 as many studies have demonstrated aberrant phosphorylation and signaling in cancer.
My lab is interested in 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 differences in PTM abundance and thermal stability and characterize how these PTMs affect protein function and contribute to cancer phenotypes. My lab is currently investigating protein phosphorylation in models of Alk resistance in non-small cell lung cancer, liposarcoma, and will soon be working with Ewing sarcoma, as well as cysteine oxidation in an aging model of non-small cell lung cancer.