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

被引：62

作者：

Tomita, T ^{[1
]}

Katayama, R ^{[1
]}

Takikawa, R ^{[1
]}

Iwatsubo, T ^{[1
]}

机构：

[1] Univ Tokyo, Grad Sch Pharmaceut Sci, Dept Neuropathol & Neurosci, Tokyo 1130033, Japan

来源：

FEBS LETTERS | 2002年 / 520卷 / 1-3期

关键词：

nicastrin; presenilin; gamma-secretase; Alzheimer's disease; N-glycosylation;

D O I：

10.1016/S0014-5793(02)02802-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The transmembrane glycoprotein nicastrin is a component of presenilin (PS) protein complex that is involved in gamma-cleavage of betaAPP 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. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：117 / 121

页数：5

共 23 条

[1] Nicastrin binds to membrane tethered Notch [J].