Abstract
β-Amyloid peptide (Aβ) is generated through the proteolytic cleavage of β-amyloid precursor protein (APP) by β- and γ-secretases. The β-secretase, BACE1, initiates Aβ formation followed by γ-cleavage within the APP transmembrane domain. Although BACE1 localizes in the transGolgi network (TGN), its physiological substrates and modulators are not known. In addition, the relationship to other secretase(s) also remains unidentified. Here, we demonstrate that BACE1 binds to nicastrin, a component of γ-secretase complexes, in vitro, and that nicastrin activates β-secretase activity in COS-7 cells.
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