Cell Biology

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Science  25 Apr 2003:
Vol. 300, Issue 5619, pp. 551
DOI: 10.1126/science.300.5619.551d

A key enzyme involved in Alzheimer's disease is known as γ-secretase. This protein complex acts as an aspartyl protease and cleaves the β-amyloid precursor protein (APP) to release amyloid β-peptide (Aβ). Several distinct membrane proteins have been identified as contributing to γ-secretase activity. Edbauer et al. have defined the minimal set of molecular components sufficient for γ-secretase activity by reconstituting this activity in yeast, chosen because it lacks any sign of γ-secretase activity and does not encode homologs of the putative γ-secretase component proteins. Human presenilin, nicastrin, APH-1, and PEN-2 together produced a holoenzyme that could faithfully reproduce β-amyloid precursor cleavage in intact yeast cells and, after detergent extraction and immunoprecipitation, in vitro.—SMH

Nature Cell Biol. 10.1038/ncb960 (2003).

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