Signal Transduction

Cell surface receptors transmit signals to the interior of the cell upon binding to a ligand. These signals are generally transmitted through proteins with catalytic activity (such as kinases) as well as those without any catalytic activity (such as adapters). Protein phosphorylation is a major mechanism of regulating the activity of these proteins and the formation of multi-protein complexes. We have cloned a number of signaling molecules that are involved in signal transduction through receptor tyrosine kinases (EGF and PDGF receptors), cytokine receptors (IL-3 and TSLP receptor), antigen receptors (T and B cell receptors), oncogenic kinases (Bcr-Abl) as well as receptor serine-threonine kinases (TGF-beta and BMP receptors). Using a combination of molecular biology and proteomics-based approaches including mass spectrometry, our laboratory aims to dissect these signaling pathways further and to elucidate the mechanisms of cross talk between them. We are developing methods to identify novel proteins involved in these signal transduction pathways in a global fashion using mass spectrometry based high-throughput methods. We are also interested in sequence databases, annotation and genomic analyses using bioinformatics to catalog all proteins and their modular domain structures and interaction partners.