The responsiveness of a cell to its environment relies on detection systems that sense changes outside the cell and are coupled to signal transduction pathways that generate appropriate cellular responses. We are interested in understanding how these systems work at the atomic level. A particular focus of our laboratory is the study of protein phosphorylation, an important chemical modification that switches the properties of signaling proteins. We study tyrosine kinases (enzymes that catalyze the transfer of phosphate from ATP to tyrosine sidechains), such as the products of the Src and Abl oncogenes, Ser/Thr kinases such as the receptors for transforming growth factor b (TGF b), as well as the Son of Sevenless (SOS) protein that activates Ras, a small GTP-binding protein that is an important signaling switch.
of the projects we are engaged in are described below:
Some of the projects we are engaged in are described below: