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- W2022278464 abstract "Activation of mammalian Notch receptor by its ligands induces TNFα-converting enzyme–dependent ectodomain shedding, followed by intramembrane proteolysis due to presenilin (PS)-dependent γ-secretase activity. Here, we demonstrate that a new modification, a monoubiquitination, as well as clathrin-dependent endocytosis, is required for γ-secretase processing of a constitutively active Notch derivative, ΔE, which mimics the TNFα-converting enzyme–processing product. PS interacts with this modified form of ΔE, ΔEu. We identified the lysine residue targeted by the monoubiquitination event and confirmed its importance for activation of Notch receptor by its ligand, Delta-like 1. We propose a new model where monoubiquitination and endocytosis of Notch are a prerequisite for its PS-dependent cleavage, and discuss its relevance for other γ-secretase substrates." @default.
- W2022278464 created "2016-06-24" @default.
- W2022278464 creator A5017978114 @default.
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- W2022278464 date "2004-07-05" @default.
- W2022278464 modified "2023-10-18" @default.
- W2022278464 title "Monoubiquitination and endocytosis direct γ-secretase cleavage of activated Notch receptor" @default.
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- W2022278464 doi "https://doi.org/10.1083/jcb.200310098" @default.
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