Phosphorylation of presenilin 1 at the caspase recognition site regulates its proteolytic processing and the progression of apoptosis.

@article{Fluhrer2004PhosphorylationOP,
  title={Phosphorylation of presenilin 1 at the caspase recognition site regulates its proteolytic processing and the progression of apoptosis.},
  author={Regina Fluhrer and Arno Friedlein and Christian Haass and Jochen Walter},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 3},
  pages={1585-93}
}
The Alzheimer's disease-associated presenilin (PS) 1 is intimately involved in gamma-secretase cleavage of beta-amyloid precursor protein and other proteins. In addition, PS1 plays a role in beta-catenin signaling and in the regulation of apoptosis. Here we demonstrate that phosphorylation of PS1 is regulated by two independent signaling pathways involving protein kinase (PK) A and PKC and that both kinases can directly phosphorylate the large hydrophilic domain of PS1 in vitro and in cultured… CONTINUE READING

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