Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo.

@article{GuillozetBongaarts2006PseudophosphorylationOT,
  title={Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo.},
  author={Angela L. Guillozet-Bongaarts and Michael E Cahill and Vincent L Cryns and Matthew R. Reynolds and Robert W. Berry and Lester I. Binder},
  journal={Journal of neurochemistry},
  year={2006},
  volume={97 4},
  pages={1005-14}
}
The tangles of Alzheimer's disease (AD) are comprised of the tau protein displaying numerous alterations, including phosphorylation at serine 422 (S422) and truncation at aspartic acid 421 (D421). Truncation at the latter site appears to result from activation of caspases, a class of proteases that cleave specifically at aspartic acid residues. It has been proposed that phosphorylation at or near caspase cleavage sites could regulate the ability of the protease to cleave at those sites. Here… CONTINUE READING
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