Reconstitution of γ-secretase activity

By D. Edbauer, E. Winkler, J. Regula, B. Pesold, H. Steiner, Christian Haass. Nature Cell Biology, 2003

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Alzheimer’s disease: pathogenesis, diagnostics, and therapeutics (2019, background): “Psen2 facilitates the maturation of PSEN, whereas Aph1 stabilizes the complex.(35) Nicastrin acts as a receptor for γ-secretase substrates.”
Different cofactor activities in γ-secretase assembly (2003, background): “Similarly, Edbauer et al. (2003) have recently reported equivalent results by coexpressing mammalian -secretase components in yeast.”
Trafficking and proteolytic processing of APP. (2012, background): “These four components are necessary and sufficient for full g-secretase activity (Edbauer et al. 2003).”
Macroautophagy—a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease (2005, background): “Both -site APP cleaving enzyme and -secretase, which is a protein complex containing presenilin (PS), nicastrin, PEN2, and Aph-1 (Edbauer et al., 2003), reside in one or more compartments of the central vacuolar apparatus, which includes the ER–Golgi, plasma membrane, endosomes, and lysosomes…”
Autophagy, amyloidogenesis and Alzheimer disease (2007, background): “The - cleavage of APP is mediated by a -secretase complex composed of the proteins presenilin (PS), nicastrin, APH1 and PEN2 (St George-Hyslop, 2000; Edbauer et al., 2003; Go et al., 2004).”