Journal
NATURE CELL BIOLOGY
Volume 5, Issue 5, Pages 486-488Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb960
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gamma-Secretase is a membrane protein complex with an unusual aspartyl protease activity that catalyses the regulated intramembranous cleavage of the beta-amyloid precursor protein (APP) to release the Alzheimer's disease (AD)-associated amyloid beta-peptide (Abeta) and the APP intracellular domain (AICD)(1). Here we show the reconstitution of gamma-secretase activity in the yeast Saccharomyces cerevisiae, which lacks endogenous gamma-secretase activity. Reconstituted gamma-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 Abeta and AICD in vitro. Thus, the biological activity of gamma-secretase is reconstituted by the co-expression of human PS, Nct, APH-1 and PEN-2 in yeast.
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