The binding and phosphorylation of Thr231 is critical for Tau's hyperphosphorylation and functional regulation by glycogen synthase kinase 3beta.

@article{Lin2007TheBA,
  title={The binding and phosphorylation of Thr231 is critical for Tau's hyperphosphorylation and functional regulation by glycogen synthase kinase 3beta.},
  author={Yuh-Te Lin and J Cheng and Li-ching Liang and Chiung-Yuan Ko and Y. Lo and Pei-Jung Frank Lu},
  journal={Journal of neurochemistry},
  year={2007},
  volume={103 2},
  pages={802-13}
}
Neuropathological hallmarks of Alzheimer's disease are extracellular senile plaques and intracellular neurofibrillary lesions. The neurofibrillary lesions mainly consist of the hyperphosphorylated microtubule-associated protein Tau predominantly expressed in the axon of CNS neurons. Hyperphosphorylation of Tau negatively affects its binding to tubulin and decreases the capacity to promote microtubule assembly. Among a number of proline-directed kinases capable of phosphorylating paired helical… CONTINUE READING
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