Ph.D. Student
Vanderbilt University Medical Center
Department of Cell & Developmental Biology
Email: kristin.e.kalie@vanderbilt.edu
Erie, PA
B.S. Molecular biology/ Biotechnology
Clarion University, Clarion, PA 2003
In the current model of Wnt signaling, binding of Wnt ligands to Frizzled-LRP5/6 co-receptor family members transmits an intracellular signal that increases steady-state levels of cytoplasmic beta-catenin. Beta-catenin then translocates to the nucleus and induces target gene expression. A major question in the field is how a Wnt signal is transmitted from the receptor to activate the pathway's intracellular components. The Frizzled receptor is predicted to have seven transmembrane domains, a feature that is characteristic of G protein-coupled receptors. Whether or not G proteins participate in Wnt signaling, however, has been controversial. We are now taking a biochemical approach to determine the role of G protein signaling in Wnt signal transduction.