GGA1-mediated endocytic traffic of LR11/SorLA alters APP intracellular distribution and amyloid-β production

• Type of Material: Article
• Authors: Jeremy H. Herskowitz, Emory University; Katrin Offe, Emory University; Aniruddha Deshpande, Emory University; Richard A Kahn, Emory University; Allan I Levey, Emory University; James J Lah, Emory University
• Language: English
• Date: 2012-07-15
• Publisher: The American Society for Cell Biology
• Publication Version: Final Published Version
• Copyright Statement: © 2012 Herskowitz et al.
• License: Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported
• Final Published Version (URL): http://dx.doi.org/10.1091%2Fmbc.E12-01-0014
• Title of Journal or Parent Work: Molecular Biology of the Cell
• Volume: 23
• Issue: 14
• Start Page: 2645
• End Page: 2657
• Grant/Funding Information: We acknowledge the donors of Alzheimer's Disease Research, a program of the American Health Assistance Foundation, for support of this research.; This work was supported by grants from the National Institutes of Health through the Emory NINDS Neuroscience Core Facilities (P30 NS055077), Alzheimer's Disease Research Center Grant AG025688, NINDS Training and Translational Research in Neurology Grant T32 NS007480-07 (J.H.H.), and Grants NIA P01AG1449 and R01GM067226 (R.A.K.).
• Research Categories: Biology, Cell; Chemistry, Biochemistry

Abstract

Defining the cellular pathway(s) by which LR11 modulates amyloid-β peptide production is critical to understanding how changes in LR11 expression affect the progression of Alzheimer's disease. These results suggest that endocytic traffic of LR11, facilitated by GGA1, enhances LR11 modulation of amyloid precursor protein processing in a nonamyloidogenic manner.