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Complex N ‐glycosylated form of nicastrin is stabilized and selectively bound to presenilin fragments
Author(s) -
Tomita Taisuke,
Katayama Ryohei,
Takikawa Rie,
Iwatsubo Takeshi
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02802-8
Subject(s) - nicastrin , presenilin , cleavage (geology) , glycosylation , glycoprotein , chemistry , biochemistry , n linked glycosylation , glycan , biology , medicine , alzheimer's disease , paleontology , disease , fracture (geology)
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.