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          Institute: MPI für molekulare Zellbiologie und Genetik     Collection: MPI-CBG Publications 2016 (archival)     Display Documents



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ID: 732387.0, MPI für molekulare Zellbiologie und Genetik / MPI-CBG Publications 2016 (archival)
The lipidome associated with the γ-secretase complex is required for its integrity and activity.
Authors:Ayciriex, Sophie; Gerber, Hermeto; Osuna, Guillermo M Garcia; Chami, Mohamed; Stahlberg, Henning; Shevchenko, Andrej; Fraering, Patrick C
Date of Publication (YYYY-MM-DD):2016
Title of Journal:The Biochemical Journal
Volume:473
Issue / Number:3
Start Page:321
End Page:334
Copyright:not available
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:γ-Secretase is a multi-subunit membrane protease complex that catalyses the final intramembrane cleavage of the β-amyloid precursor protein (APP) during the neuronal production of amyloid-β peptides (Aβ), which are implicated as the causative agents of Alzheimer's disease (AD). In the present study, we report the reconstitution of a highly purified, active γ-secretase complex into proteoliposomes without exogenous lipids and provide the first direct evidence for the existence of a microenvironment of 53 molecular species from 11 major lipid classes specifically associated with the γ-secretase complex, including phosphatidylcholine and cholesterol. Importantly, we demonstrate that the pharmacological modulation of certain phospholipids abolishes both the integrity and the enzymatic activity of the intramembrane protease. Together, our findings highlight the importance of a specific lipid microenvironment for the structure and function of γ-secretase.
External Publication Status:published
Document Type:Article
Version Comment:Automatic journal name synchronization
Communicated by:Thüm
Affiliations:MPI für molekulare Zellbiologie und Genetik
Identifiers:LOCALID:6432
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