Research

Our broad research interest is in understanding how post-translational modifications modulate the properties of proteins. Specifically, we study "nutrient sensing" by characterizing the enzymes O-GlcNAc transferase, O-GlcNAcase, mTOR (mammalian target of Rapamycin, a ser-thr kinase), and AMP-activated protein kinase in mammalian cell culture and animal tissues. These enzymes have been implicated in responding to nutrients and regulating signal transduction cascades. Using a combination of methodologies, including mass spectrometry, protein biochemistry, cell biology, proteomics, and molecular biology, we plan to further elucidate the mechanisms by which cells recognize their environment.

Our research is aimed at building on a model in which cells are not blindly responding to extracellular stimuli but instead are taking into account their own nutritional states and then responding appropriately. The goal is that elucidation of this model will help to convert a simple "ON/OFF" Newtonian model of extracellular stimuli-mediated signal transduction into a quantum probability model of cells integrating both extra- and intracellular signaling information before responding to environmental cues. The hope is that this paradigm shift will not only more accurately describe fundamental biological processes but will also elucidate novel therapeutic targets in disease states such as type II diabetes and cancer.