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• W2034193841 abstract "The gamma-secretase complex is required for intramembrane cleavage of several integral membrane proteins, including the Notch receptor, where it generates an active signaling fragment. Four putative gamma-secretase components have been identified-presenilin (Psn), nicastrin (Nct), Aph-1, and Pen-2. Here, we use a stepwise coexpression approach to investigate the role of each new component in gamma-secretase assembly and activation. Coexpression of all four proteins leads to high level accumulation of mature Psn and increased proteolysis of Notch. Aph-1 and Nct may form a subcomplex that stabilizes the Psn holoprotein at an early step in gamma-secretase assembly. Subcomplex levels of Aph-1 are down-regulated by stepwise addition of Psn, suggesting that Aph-1 might not enter the mature complex. In contrast, Pen-2 accumulates proportionally with Psn, and is associated with Psn endoproteolysis during gamma-secretase assembly. These results demonstrate that Aph-1 and Pen-2 are essential cofactors for Psn, but that they play different roles in gamma-secretase assembly and activation." @default.
• W2034193841 created "2016-06-24" @default.
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• W2034193841 date "2003-05-26" @default.
• W2034193841 modified "2023-10-12" @default.
• W2034193841 title "Different cofactor activities in γ-secretase assembly" @default.
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• W2034193841 doi "https://doi.org/10.1083/jcb.200304014" @default.
• W2034193841 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2199374" @default.
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