Structural biology of intramembrane proteases: mechanistic insights from rhomboid and S2P to γ-secretase

Current Opinion in Structural Biology
Linfeng SunYigong Shi

Abstract

Intramembrane proteases catalyze hydrolysis of peptide bond within the lipid bilayer and play a key role in a variety of cellular processes. These membrane-embedded enzymes comprise four major classes: rhomboid serine proteases, site-2 metalloproteases, Rce1-type glutamyl proteases, and aspartyl proteases exemplified by signal peptide peptidase and γ-secretase. In the past several years, three-dimensional structures of representative members of these four classes of intramembrane protease have been reported at atomic resolutions, which reveal distinct protein folds and active site configurations. These structures, together with structure-guided biochemical analyses, shed light on the working mechanisms of water access and substrate entry. In this review, we discuss the shared as well as unique features of these intramembrane proteases, with a focus on presenilin-the catalytic component of γ-secretase.

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Citations

May 4, 2016·Journal of Neuroimmune Pharmacology : the Official Journal of the Society on NeuroImmune Pharmacology·Roman M LevytskyyOleh Khalimonchuk
Sep 4, 2018·Journal of Biomolecular Structure & Dynamics·Hua ZhouXuri Huang
Aug 17, 2019·Journal of Cell Science·Nathalie KühnleMarius K Lemberg
Aug 14, 2019·Journal of Biomolecular Structure & Dynamics·Budheswar DehuryKasper P Kepp
Jul 9, 2016·Biological Chemistry·Kunihiko Kanatsu, Taisuke Tomita
Oct 2, 2019·Nature Structural & Molecular Biology·Sangwoo ChoSiniša Urban
Jun 9, 2020·Frontiers in Molecular Neuroscience·Xinyue LiuChunyu Wang
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Aug 19, 2017·Expert Opinion on Therapeutic Targets·Kohji Moriishi
Mar 30, 2018·Current Opinion in Structural Biology·Charles R Sanders, James M Hutchison
Apr 19, 2021·The Journal of Biological Chemistry·Tatsuhiko YokoyamaYoshinori Akiyama
Jun 3, 2021·International Journal of Molecular Sciences·Francesca TosettiMaria Raffaella Zocchi

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