The effect of phosphorylation on the structure and function of the microtubule associated protein Tau
I grew up in Kingston, Jamaica before moving to the States. In May 2011 I graduated with my BS in Biology, Microbiology option from Virginia Tech and in the fall of 2012 I joined the CMB Program. So far I’ve enjoyed all the new experiences that Vermont and the Program have afforded. Outside the lab I like to swim, cook and explore.
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.
Office: E217A Given
Lab: E215 Given
- 12/17/2013 11:30 AM – 12:30 PM
- 1/28/2014 11:30 AM – 12:30 PM
- 2/4/2014 11:30 AM – 12:30 PM
Dr. Andrew McKenzie
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