The neuronal microtubule associated protein, Tau plays an important role in the transport of cargo through the axon. While Tau is extensively studied in the development of neurodegenerative disease, my research is focused on Tauâ€™s normal activity and how phosphorylation controls Tauâ€™s behavior, structure and function on the microtubule surface. Outside of lab I enjoy reading, cooking and exploring the outdoors. Vermont is a great place to find new books, fresh ingredients and beautiful places.
Lab GroupA member of the Christopher Berger Laboratory
Tau is a neuronal microtubule associated protein that participates in a number of processes including stabilizing microtubules (MTs), interacting with the actin cytoskeleton, participating in signaling cascades and inhibiting kinesin-1 mediated motor transport in vitro. In Alzheimer's Disease, Tau is hyperphosphorylated and is a major component of neurofibrillary tangles which have been shown to disrupt fast axonal transport. Though there is much emphasis placed on Tau in the disease state, we believe that Tau's function in the non-disease state should be elucidated so that we can better understand the changes that lead to disease. To that end, my project looks at phosphorylation of tyrosine 18 of Tau and the effect this has on Tau's dynamic structure and its ability to bind to the MT, inhibit kinesin-1 run length and participate in signaling cascades involving protein phosphatase 1 and glycogen synthase kinase-3.