A ubiquitin-binding CUE domain in presenilin-1 enables interaction with K63-linked polyubiquitin chains

FEBS Letters
Stephen P DugganJustin V McCarthy

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.

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Citations

Oct 27, 2015·Cellular Signalling·Stephen P Duggan, Justin V McCarthy
Sep 28, 2015·Trends in Cell Biology·Dönem Avci, Marius K Lemberg
Oct 29, 2017·Biochemical Society Transactions·Aonghus J McCarthyJustin V McCarthy
Mar 3, 2019·Cells·Naoto Oikawa, Jochen Walter
Dec 2, 2015·Molecular Psychiatry·J I VélezM Arcos-Burgos

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