Christian Carter-Su


Christian Carter-Su, PhD, received her BS degree in 1972 in Applied Mathematics-Biomedical Sciences from Brown University, where she did mathematical modeling of glucose homeostasis in humans. She obtained her PhD in biophysics in 1978 from the University of Rochester, where she studied the energetics of sodium-dependent glucose and amino acid transport in the intestine. Her postdoctoral research was on insulin regulation of glucose transport in fat cells in the laboratory of Dr. Michael Czech at Brown University. In 1981, she joined the Department of Physiology at the University of Michigan Medical School where she currently holds the titles of Henry Sewall Collegiate Professor of Physiology, Anita H. Payne Distinguished University Professor, Professor of Internal Medicine, and Associate Director of the Michigan Diabetes Research Center. Over her career, she has received a number of awards recognizing her research and/or mentoring, including the Roy O. Greep Award for outstanding contributions to research in endocrinology from the Endocrine Society and the Bodil M. Schmidt-Nielsen Distinguished Mentor and Scientist Award from The American Physiological Society.

Dr. Carter-Su’s research over the past 30+ years has focused on defining the signal transduction events that are initiated upon growth hormone (GH) binding to its receptor that lead to its diverse effects on growth and metabolism. In 1993, her laboratory made the seminal discovery that the GH receptor is associated with the tyrosine kinase JAK2. Further, GH binding to its receptor activates JAK2 and stimulates the phosphorylation of multiple tyrosines within JAK2 and the GH receptor. Because phosphorylated tyrosines can recruit signaling proteins, this provided the first insight into how GH might elicit its diverse cellular responses. Since that time, her laboratory has used a large variety of approaches to determine what tyrosines in proteins are phosphorylated in JAK2 and GH receptor, what proteins are recruited to JAK2/GH receptor complexes in response to ligand activation (e.g. Stat transcription factors, IRS proteins), what signaling pathways and cell processes are initiated or regulated as a consequence of the recruitment of these proteins to the JAK2/GH receptor complex (e.g. the MAP kinase pathway), and how JAK2 is activated and subsequently inactivated by ligand binding. Her current research focuses on the function of one of the novel JAK2-interacting proteins identified – the scaffold protein SH2B1. SH2B1 is recruited to activated JAK2 and a number of activated receptor tyrosine kinases. Both human and mouse studies suggest that SH2B1 is a major regulator of body weight, insulin sensitivity, and behavior. At the cellular level, her lab has shown SH2B1 to enhance ligand-induced gene expression, neurite outgrowth, and cell motility.