Our lab is interested in the functional interactions of membrane proteins with their environment and with cytosolic adaptor proteins. The principal project examines the mechanisms by which the LDL receptor binds, internalizes and delivers lipoproteins in cells. Studies under this project include mapping the lipoprotein binding surfaces on the LDL receptor, identifying and characterizing the cytosolic components that mediate receptor-lipoprotein internalization, and characterizing the mechanisms by which the receptor delivers lipoproteins to endosomes. A second project examines protein structure and function associated with repeating motifs in proteins of the membrane skeleton. The membrane skeleton is a cytoskeletal network that provides structural support cellular membranes and modulates membrane function. The two most common protein motifs in this cytoskeleton are spectrin repeats and ANK repeats. Both motifs form structures that can function as mechanical springs. Current work on this project is directed toward using designed ANK repeat proteins as nanosprings in the development of shear sensitive nanodevices.