Professor Adam W. Smith of the University of Akron

"Resolving the receptor tyrosine kinase interactions in live cells and the effect of oncogenic mutations"

The plasma membrane is a complex boundary between the cell and its surroundings. Cells have an array of protein receptors on the plasma membrane that help process environmental cues. The spatial and temporal arrangement of these receptors is critical to function, but the chemical forces driving this organization are not well understood. In my lab, we develop and apply a variety of fluorescence assays to measure membrane protein interactions in situ. This talk will focus on receptor tyrosine kinases (RTKs), which are transmembrane proteins that regulate cell growth, proliferation, and differentiation. Several RTKs are oncogenic and are targeted in next generation anti-cancer drug development. My lab has resolved functionally important interfaces in RTKs using pulsed interleaved excitation fluorescence cross-correlation spectroscopy (PIE-FCCS). PIE-FCCS is especially powerful because it is sensitive to protein mobility, concentration, and monomer/dimer/oligomer distributions. I will describe ongoing work in my group to investigate two RTKS: EGFR and EphA2.