Author: ["Dieter Edbauer","Edith Winkler","Joerg T. Regula","Brigitte Pesold","Harald Steiner","Christian Haass"]
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Abstract
γ-Secretase is a membrane protein complex with an unusual aspartyl protease activity that catalyses the regulated intramembranous cleavage of the β-amyloid precursor protein (APP) to release the Alzheimer's disease (AD)-associated amyloid β-peptide (Aβ) and the APP intracellular domain (AICD)1. Here we show the reconstitution of γ-secretase activity in the yeast Saccharomyces cerevisiae, which lacks endogenous γ-secretase activity. Reconstituted γ-secretase activity depends on the presence of four complex components including presenilin (PS)1, nicastrin (Nct)2, APH-1 (refs 3–6) and PEN-2 (refs 4, 7), is associated with endoproteolysis of PS8, and produces Aβ and AICD in vitro. Thus, the biological activity of γ-secretase is reconstituted by the co-expression of human PS, Nct, APH-1 and PEN-2 in yeast.Cite this article
Edbauer, D., Winkler, E., Regula, J. et al. Reconstitution of γ-secretase activity. Nat Cell Biol 5, 486–488 (2003). https://doi.org/10.1038/ncb960 