Protein phosphorylation by kinases is an important regulatory modification that controls many cellular processes. Advances in tools and approaches to study this modification have greatly expanded the catalog of known phosphorylation sites but there remain substantial gaps in our knowledge. We will apply novel kinome- centric analyses to study canonical cell signaling pathways in order to define pathway-specific signaling modules. Our goal is to develop a mass spectrometry-based phenotyping assay that can identify phosphosignatures of cell signaling.
Our cells use protein phosphorylation to control signaling networks in many cellular processes, both in health and disease. We only know the functional relevance of <3% of phosphorylation sites and powerful analytical methods that constantly expand the catalog of known sites are drastically outpacing our ability to study these important protein modifications. Using novel tools, we will thoroughly characterize cell signaling pathways to learn the most functionally important phosphorylation sites, enabling the development of sensitive and specific clinical diagnostics.