Complex N-glycosylated form of nicastrin is stabilized and selectively bound to presenilin fragments.

@article{Tomita2002ComplexNF,
  title={Complex N-glycosylated form of nicastrin is stabilized and selectively bound to presenilin fragments.},
  author={Taisuke Tomita and Ryohei Katayama and Rie Takikawa and Takeshi Iwatsubo},
  journal={FEBS letters},
  year={2002},
  volume={520 1-3},
  pages={
          117-21
        }
}
The transmembrane glycoprotein nicastrin is a component of presenilin (PS) protein complex that is involved in gamma-cleavage of beta APP and site-3 cleavage of Notch. PS undergoes endoproteolysis, and the proteolytic fragments are incorporated into the high molecular weight protein complexes that are highly stabilized. Here we show that Endo H-resistant, N-glycosylated form of nicastrin (p150-NCT) is highly stabilized and selectively bound to PS fragments. Moreover, loss-of-function mutations… CONTINUE READING
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