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    FEBS Lett. 2002 Jun 5;520(1-3):117-21.

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

    Tomita T, Katayama R, Takikawa R, Iwatsubo T.

    Department of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo, Tokyo 113-0033, Japan. taisuke@mol.f.u-tokyo.ac.jp

    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 of nicastrin inhibited formation of fully glycosylated p150-NCT as well as stabilization of nicastrin, suggesting that glycosylation and stabilization of nicastrin polypeptides are tightly correlated with its function.

    PMID: 12044882 [PubMed - indexed for MEDLINE]

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