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- W2022330109 endingPage "20637" @default.
- W2022330109 startingPage "20630" @default.
- W2022330109 abstract "BACE1 is a type I transmembrane aspartyl protease that cleaves amyloid precursor protein at the β-secretase site to initiate the release of β-amyloid peptide. As a secretase, BACE1 also cleaves additional membrane-bound molecules by exerting various cellular functions. In this study, we showed that BACE1 can effectively shed the membrane-anchored signaling molecule Jagged 1 (Jag1).Wealso mapped the cleavage sites of Jag1 by ADAM10 and ADAM17. Although Jag1 shares a high degree of homology with Jag2 in the ectodomain region, BACE1 fails to cleave Jag2 effectively, indicating a selective cleavage of Jag1. Abolished cleavage of Jag1 in BACE1-null mice leads to enhanced astrogenesis and, concomitantly, reduced neurogenesis. This characterization provides biochemical evidence that the Jag1-Notch pathway is under the control of BACE1 activity" @default.
- W2022330109 created "2016-06-24" @default.
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- W2022330109 date "2014-07-01" @default.
- W2022330109 modified "2023-10-16" @default.
- W2022330109 title "β-Site Amyloid Precursor Protein Cleaving Enzyme 1(BACE1) Regulates Notch Signaling by Controlling the Cleavage of Jagged 1 (Jag1) and Jagged 2 (Jag2) Proteins" @default.
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- W2022330109 doi "https://doi.org/10.1074/jbc.m114.579862" @default.
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- W2022330109 hasPublicationYear "2014" @default.
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