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Yohan Kim

Mentor: Gloria Lee, Ph.D.
Lab Room: B191 ML
Lab Phone: 319-335-8656

Identification of functions for abnormally phosphorylated Tau

The microtubule-associated protein Tau is involved in regulating microtubule assembly and function in neurons. During early development of brain, Tau is phosphorylated on sites such as Tyr-18, Tyr-29, Thr-231, and Ser-262. Our lab is interested in the function of these phospho-sites since they also appear in Alzheimer’s disease (AD). Upon NGF stimulation, developing neuronal cells differentiate through MAPK activation and we have found that MAPK activation is potentiated by Tau. In addition, we found that phosphorylation of Tau at Thr-231, which reduces its affinity for microtubules, is required for Tau to potentiate MAPK activation and that phospho-Thr231-Tau is associated with SHP-2, a protein tyrosine phosphatase that is important in NGF signaling. In our research project, we are focusing on the function of the phospho-Thr231-Tau – SHP-2 interaction and how it contributes to NGF signaling. Since phospho-Thr231-Tau is also present in AD, we expect that our research would help understand not only functions of Tau in early development but also signal transduction activated during neuropathogenesis.