Maurine Linder Back to Faculty Listing Page . . . . . . . . . . . . . . . . Numerous signaling proteins, including heterotrimeric G proteins, Ras proteins, and nonreceptor tyrosine kinases, reside on the cytoplasmic face of the plasma membrane where they are poised to receive signals from cell surface receptors. Association of these molecules with membranes and their functional activities rely on the covalent attachment of lipids, including reversible acylation with palmitate. Our goal is to understand how regulated palmitoylation affects subcellular location and protein-protein interactions of signaling proteins.
Current research is focused on the following questions.
Using biochemical and genetic approaches, we seek to define the molecular basis of a palmitoyltransferase activity present in plasma membranes. The pheromone response pathway in yeast is used as a model to study the physiological significance of palmitoylation of G protein subunits. A second line of investigation centers on palmitoylated proteins in the nerve terminal. RGS4 binds to membranes through an amphipathic alpha-helix. Manahan CL, Patnana M, Blumer KJ, et al.