Presenilin-1 affects trafficking and processing of βAPP and is targeted in a complex with nicastrin to the plasma membrane

@article{Kaether2002Presenilin1AT,
  title={Presenilin-1 affects trafficking and processing of βAPP and is targeted in a complex with nicastrin to the plasma membrane},
  author={Christoph Kaether and Sven Lammich and Dieter Edbauer and Michaela Ertl and Jens Rietdorf and Anja Capell and Harald Steiner and Christian Haass},
  journal={The Journal of Cell Biology},
  year={2002},
  volume={158},
  pages={551 - 561}
}
Amyloid beta-peptide (Abeta) is generated by the consecutive cleavages of beta- and gamma-secretase. The intramembraneous gamma-secretase cleavage critically depends on the activity of presenilins (PS1 and PS2). Although there is evidence that PSs are aspartyl proteases with gamma-secretase activity, it remains controversial whether their subcellular localization overlaps with the cellular sites of Abeta production. We now demonstrate that biologically active GFP-tagged PS1 as well as… CONTINUE READING