| Literature DB >> 24373285 |
Vinod Udayar1, Virginie Buggia-Prévot2, Rita L Guerreiro3, Gabriele Siegel4, Naresh Rambabu5, Amanda L Soohoo6, Moorthi Ponnusamy5, Barbara Siegenthaler4, Jitin Bali7, Mikael Simons8, Jonas Ries9, Manojkumar A Puthenveedu6, John Hardy3, Gopal Thinakaran2, Lawrence Rajendran10.
Abstract
Alzheimer's disease (AD) is characterized by cerebral deposition of β-amyloid (Aβ) peptides, which are generated from amyloid precursor protein (APP) by β- and γ-secretases. APP and the secretases are membrane associated, but whether membrane trafficking controls Aβ levels is unclear. Here, we performed an RNAi screen of all human Rab-GTPases, which regulate membrane trafficking, complemented with a Rab-GTPase-activating protein screen, and present a road map of the membrane-trafficking events regulating Aβ production. We identify Rab11 and Rab3 as key players. Although retromers and retromer-associated proteins control APP recycling, we show that Rab11 controlled β-secretase endosomal recycling to the plasma membrane and thus affected Aβ production. Exome sequencing revealed a significant genetic association of Rab11A with late-onset AD, and network analysis identified Rab11A and Rab11B as components of the late-onset AD risk network, suggesting a causal link between Rab11 and AD. Our results reveal trafficking pathways that regulate Aβ levels and show how systems biology approaches can unravel the molecular complexity underlying AD.Entities:
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Year: 2013 PMID: 24373285 PMCID: PMC4004174 DOI: 10.1016/j.celrep.2013.12.005
Source DB: PubMed Journal: Cell Rep Impact factor: 9.423