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- W2023490024 abstract "γ–Secretase is involved in the production of amyloid β–peptide, the principal component of amyloid plaques in the brains of Alzheimer's disease patients. γ–Secretase is a complex composed of presenilin, nicastrin, Aph1 and Pen2. We previously proposed a mechanism of complex assembly by which unassembled subunits are retained in the ER and only the fully assembled complex is exported from the ER (EMBO J 23, 4738–48). We now wanted to analyze the retention mechanism of the γ–secretase subunit Pen2. Using reporter proteins for membrane trafficking, deglycosylation experiments and co–immunoprecipitations, we show that unassembled Pen2 is retained in the ER by Rer1, a putative ER–retention/retrieval protein. Direct binding of unassembled Pen2 to Rer1 is mediated by the first transmembrane domain of Pen2 and a conserved asparagine in this domain is required. Our data suggest that unassembled Pen2 is retained in the ER via a signal in its first transmembrane domain that binds Rer1. Rer1 is part of a quality control system that ensures that only fully assembled γ–secretase is exported from the ER." @default.
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- W2023490024 date "2006-07-01" @default.
- W2023490024 modified "2023-09-26" @default.
- W2023490024 title "O1-02-02: Er-retention and complex assembly of the γ-secretase component Pen2 are mediated by its first transmembrane domain and interaction with Rer1" @default.
- W2023490024 doi "https://doi.org/10.1016/j.jalz.2006.05.254" @default.
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