Abstract
Results: We found that pseudophosphorylated tau aggregates in cells when Thr 212 is mutated to Glu (Ps-tau), suggesting that phosphorylation at this site facilitates tau self-assembly. The expression of tau pseudophosphorylated at Thr212, Thr231, and Ser262 disrupts the microtubules when co-transfected with fluorescent tubulin. EB-1 is a protein that binds to the growing end of the microtubules. Cells stably transfected with fluorescent EB-1 are used to visualize the dynamics of these filaments in the live cells. These cells were transfected with an inducible system to express tau upon withdraw of doxycycline (TET-off). The effect of Ps-tau on these cells was also studied. Conclusions: These findings suggest that tau phosphorylation at Thr 212 facilitates tau self-aggregation, and that the combination of phosphorylation at Thr212, 231 and Ser262 in the same tau molecule can trigger toxic reaction.
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