Protein phosphorylation regulates relative utilization of processing pathways for Alzheimer beta/A4 amyloid precursor protein.

@article{Gandy1993ProteinPR,
  title={Protein phosphorylation regulates relative utilization of processing pathways for Alzheimer beta/A4 amyloid precursor protein.},
  author={Sam Gandy and Gregg L Caporaso and Joseph D. Buxbaum and O de Cruz Silva and Kerstin Iverfeldt and Christer Nordstedt and Toshiharu Suzuki and Andrew J. Czernik and Angus C. Nairn and Paul Greengard},
  journal={Annals of the New York Academy of Sciences},
  year={1993},
  volume={695},
  pages={117-21}
}
The Alzheimer amyloid precursor protein (APP) is a phosphoprotein, and the phosphorylation state of APP at Ser655 can be regulated by protein kinase C, calcium/calmodulin-dependent protein kinase II, and okadaic acid-sensitive protein phosphatases. Other enzymes may also play a role at Ser655 of APP and, perhaps, at other residues. Signal transduction via protein phosphorylation regulates APP metabolism. In particular, APP processing via the nonamyloidogenic secretory cleavage pathway is… CONTINUE READING