Karen L. Hinkle completed her Ph.D. in physiology at the University of Michigan in Ann Arbor and her B.S. in animal physiology and neuroscience at UC San Diego.
She’s had an active research program since her arrival at Norwich, mentoring over 25 undergraduate and high school students in her laboratory, publishing in peer-reviewed journals alongside undergraduate authors, presenting at national and regional conferences, and obtaining over $200K in grant funds. Her work focuses on understanding “molecular switches,” or phosphorylation sites, on proteins involved in normal development but also implicated in cancer. She and her students actively collaborate with Bryan Ballif, a professor at the University of Vermont.
Our lab studies the fundamental intracellular signaling networks that govern how cells grow. Proteins are the macromolecules that are primarily responsible for cellular functions (growth, migration, differentiation, metabolism, etc.), and proteins mediate these functions by interacting with each other in complicated networks (similar to how you might envision social networks where each individual represents a protein). Since these networks are so complicated, it takes significant effort and a variety of methods to understand protein-protein binding relationships that are involved in specific pathways that might be important for a variety of biological responses, including development and growth.
My students and I are interested primarily in growth signaling networks, namely those that are related to a transmembrane protein called DCBLD2. In this NSF-funded project in collaboration with Drs. Bryan Ballif and Alicia Ebert at the University of Vermont, we’re finding that this relatively understudied protein binds to many other proteins that are already known to be important to certain normal biological pathways but also those that are implicated in aberrant growth including cancers. These binding relationships with DCBLD2 are novel, never before identified, which makes piecing together these “signaling maps” an exciting endeavor.
U250 & Jackman 309A
1 (802) 485-2341
While at Norwich, I’ve mentored over 30 students in undergraduate research projects, some which have been investigating the “DCBLD2 interactome.”
Hinkle, K.L. and D. Olsen. Exposure to the lampricide TFM elicits an environmental stress response in yeast. FEMS Yeast Research. 19(1), 2019. doi: 10.1093/femsyr/foy121; https://www.ncbi.nlm.nih.gov/pubmed/30445546
Weir M., *Z. W. Fulton, J. M. Hao, J. E. Mann, A. McGehee, T. Corwin, J. F. Maniscalco, *E. F. Chapdelaine, M. C. Kenney, K. M. Roman Roque, U. Stelzl, P. B. Deming, P. Juo, B. A. Ballif, and K. L. Hinkle. Novel Tyrosine Phosphorylation Sites Fine Tune the Activity and Substrate Binding of Src Family Kinases FEBS Lett. 590(8):1042-52, 2016. doi: 10.1002/1873-3468.12144; https://www.ncbi.nlm.nih.gov/pubmed/27001024
Hinkle, K.L., *C.C. Anderson, B. *Forkey, *J. Griffin, *K. Cone, C. Vitzthum, and D. Olsen. Exposure to the lampricide 3-trifluoromethyl-4-nitrophenol results in increased expression of carbohydrate transporters in S. cerevisiae. Environ Toxicol Chem. 35(7):1727-32, 2016. doi: 10.1002/etc.3314; https://www.ncbi.nlm.nih.gov/pubmed/26606276
Aten, T.M., M.M. Redmond, S.O. Weaver, C.C. Love, A.S. Lapp, K.L. Hinkle, and B.A. Ballif. Tyrosine Phosphorylation of the orphan receptor ESDN/DCBLD2 serves as a scaffold for the signaling adaptor CrkL. FEBS Lett.587(15):2313-8, 2013. doi: 10.1016/j.febslet.2013.05.064. https://www.ncbi.nlm.nih.gov/pubmed/23770091
Lopez-Diaz, L.*, K.L. Hinkle*, R.N. Jain, Y. Zavros, C.S. Brunkan, T. Keeley, K.A. Eaton, J.L. Merchant, C.S. Chew, and L.C. Samuelson. Parietal Cell Hyperstimulation and Autoimmune Gastritis in Cholera Toxin Transgenic Mice. Am. J. Physiol.
Gastroint. Liver Physiol. 290: G970- G979, 2006. *First authorship shared https://www.ncbi.nlm.nih.gov/pubmed/16399875
Hinkle, K. L., G. C. Bane, A. Jazayeri, and L. C. Samuelson. Enhanced Calcium Signaling and Acid Secretion in Parietal Cells from Gastrin-deficient Mice. Am J. Physiol. Gastroint. Liver Physiol. 284: G145-G153, 2003. https://www.ncbi.nlm.nih.gov/pubmed/12388185