Complex N-glycosylated form of nicastrin is stabilized and selectively bound to presenilin fragments |
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Authors: | Tomita Taisuke Katayama Ryohei Takikawa Rie Iwatsubo Takeshi |
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Institution: | 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 |
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Abstract: | 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. |
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Keywords: | Nicastrin Presenilin γ-Secretase Alzheimer’s disease N-glycosylation |
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