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- W2114689657 abstract "The presenilins (PS1 and PS2) are the catalytic component of the γ-secretase intramembrane protease complex, involved in the regulated intramembrane proteolysis of numerous type I transmembrane proteins, including amyloid precursor protein (APP) and Notch. Herein, we describe the identification and characterization of a CUE (coupling of ubiquitin conjugation to endoplasmic reticulum degradation) ubiquitin-binding domain (UBD) in PS1, and demonstrate that the CUE domain of PS1 mediates non-covalent binding to Lysine 63-linked polyubiquitin chains. Our results highlight a γ-secretase-independent function for non-covalent ubiquitin signaling in the regulation of PS1, and add new insights into the structure and function of the presenilin proteins." @default.
- W2114689657 created "2016-06-24" @default.
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- W2114689657 date "2015-03-18" @default.
- W2114689657 modified "2023-10-09" @default.
- W2114689657 title "A ubiquitin-binding CUE domain in presenilin-1 enables interaction with K63-linked polyubiquitin chains" @default.
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- W2114689657 doi "https://doi.org/10.1016/j.febslet.2015.03.008" @default.
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