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

FEBS Letters

Iwatsubo, Takeshi¹  Takikawa, Rie¹  Katayama, Ryohei¹  Tomita, Taisuke¹ 

[1] Department of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo, Tokyo 113-0033, Japan

关键词: Nicastrin;    Presenilin;    γ-Secretase;    Alzheimer's disease;    N-glycosylation;   

DOI  :  10.1016/S0014-5793(02)02802-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The transmembrane glycoprotein nicastrin is a component of presenilin (PS) protein complex that is involved in γ-cleavage of βAPP 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.

【 授权许可】

Unknown