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- W2013076799 abstract "Presenilin is a membrane-embedded intramembrane-cleaving protease with a conserved catalytic G×GD motif. It is the catalytic subunit of γ-secretase, which plays critical roles in developmental biology and the molecular etiology of Alzheimer disease, together with three membrane protein cofactors, nicastrin, Aph-1 and Pen-2. Biochemical and enzymatic analyses have revealed that γ-secretase executes two types of proteolytic activities on a single substrate; an endopeptidase-like cleavage followed by carboxypeptidase-like processive cleavage. Utilizing small molecule inhibitors/modulators together with the substituted cysteine accessibility method, we identified certain residues and regions of presenilin that contribute to the formation of a catalytic pore structure within the lipid bilayer required for its intramembrane-cleaving activity. Recently, determination of the crystal structure of the archaeal presenilin homologue has confirmed the intramembranous location of the two conserved and essential aspartates. In this review, I will introduce the recent progresses in the understanding of the molecular mechanisms of action of this atypical protease." @default.
- W2013076799 created "2016-06-24" @default.
- W2013076799 creator A5090117851 @default.
- W2013076799 date "2014-08-09" @default.
- W2013076799 modified "2023-10-18" @default.
- W2013076799 title "Molecular mechanism of intramembrane proteolysis by γ-secretase" @default.
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- W2013076799 doi "https://doi.org/10.1093/jb/mvu049" @default.
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