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.