Research in Dr. Glomset’s group was focused on the structure and function of prenylated proteins and on the structure and biogenesis of animal cell membranes. Prenylated proteins were studied in collaboration with Mike Gelb, Chemistry, with special reference to low molecular weight GTP-binding proteins. The team searched for receptors that might mediate the binding of these proteins to specific intracellular membranes. Research on structure and biogenesis of cell membranes was designed to identify mechanisms that might promote the formation of specific phospholipid domains. One of these mechanisms appears to involve metabolic pathway that forms arachidonic acid-containing phospholipids including phosphatidylinositol. The lab investigated the precise intracellular distribution of the enzymes that contribute to this pathway.
“Spreading of differentiating human monocytes is associated with a major increase in membrane-bound CDC42Hs”, Aepfelbacher, M., Vauti, F., Weber, P.C., Glomset, J.A., Proceedings of the National Academy of Sciences of the United States of America, 91, 4263 (1994).
“Arachidonoyl-diacylglycerol kinase from bovine testis: purification and properties”, Walsh, J.P., Suen, R., Lemaitre, R.N., Glomset, J.A., Journal of Biological Chemistry, 269, 21155 (1994).
“Identification of a phosphatidic acid-preferring phospholipase A1 from bovine brain and testis”, Higgs, H.N. and Glomset, J.A., Proceedings of the National Academy of Sciences of the United States of America, 91, 9574 (1994).
“Role of protein lipidation reactions in programming interactions between ras-related GTPases and cell membranes”, Glomset, J.A., Farnsworth, C.C., Annual Review of Cell Biology, 10, 191 (1994).
“Lecithin:cholesterol acyltransferase deficiency and fish eye disease”, Glomset, J.A., Assmann, G., Norum, K.R. In The Metabolic Basis of Inherited Disease, Seventh edition, C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle, eds. New York: McGraw-Hill Book Company, December 1994.
“Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases rab1A and rab3A”, Proceedings of the National Academy of Sciences of the United States of America, 91, 11963 (1994).