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    VPS35 Parkinson mutation impairs autophagy via WASH.
    Cell Cycle 2014 25;13(14):2155-6. Epub 2014 Jun 25.
    Department of Medical Genetics; Cambridge Institute for Medical Research; University of Cambridge; Wellcome Trust/MRC Building; Addenbrooke's Hospital; Cambridge UK.

    Similar Publications

    Mutation in VPS35 associated with Parkinson's disease impairs WASH complex association and inhibits autophagy.
    Nat Commun 2014 May 13;5:3828. Epub 2014 May 13.
    Department of Medical Genetics, Cambridge Institute for Medical Research, Cambridge Biomedical Campus, University of Cambridge, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK.
    Endosomal protein sorting controls the localization of many physiologically important proteins and is linked to several neurodegenerative diseases. VPS35 is a component of the retromer complex, which mediates endosome-to-Golgi retrieval of membrane proteins such as the cation-independent mannose 6-phosphate receptor. Furthermore, retromer is also required for the endosomal recruitment of the actin nucleation promoting WASH complex. Read More
    Retromer binding to FAM21 and the WASH complex is perturbed by the Parkinson disease-linked VPS35(D620N) mutation.
    Curr Biol 2014 Jul 3;24(14):1670-1676. Epub 2014 Jul 3.
    The Henry Wellcome Integrated Signaling Laboratories, School of Biochemistry, Medical Sciences Building, University of Bristol, Bristol BS8 1TD, UK. Electronic address:
    Retromer is a protein assembly that plays a central role in orchestrating export of transmembrane-spanning cargo proteins from endosomes into retrieval pathways destined for the Golgi apparatus and the plasma membrane [1]. Recently, a specific mutation in the retromer component VPS35, VPS35(D620N), has linked retromer dysfunction to familial autosomal dominant and sporadic Parkinson disease [2, 3]. However, the effect of this mutation on retromer function remains poorly characterized. Read More
    VPS35 in Dopamine Neurons Is Required for Endosome-to-Golgi Retrieval of Lamp2a, a Receptor of Chaperone-Mediated Autophagy That Is Critical for α-Synuclein Degradation and Prevention of Pathogenesis of Parkinson's Disease.
    J Neurosci 2015 Jul;35(29):10613-28
    Departments of Neuroscience and Regenerative Medicine and Neurology, Medical College of Georgia, Georgia Regents University, Augusta, Georgia 30912, Charlie Norwood VA Medical Center, Augusta, Georgia 30912,
    Vacuolar protein sorting-35 (VPS35) is essential for endosome-to-Golgi retrieval of membrane proteins. Mutations in the VPS35 gene have been identified in patients with autosomal dominant PD. However, it remains poorly understood if and how VPS35 deficiency or mutation contributes to PD pathogenesis. Read More
    TRAPPIII is responsible for vesicular transport from early endosomes to Golgi, facilitating Atg9 cycling in autophagy.
    J Cell Sci 2013 Nov 28;126(Pt 21):4963-73. Epub 2013 Aug 28.
    Center for Frontier Oral Science, Graduate School of Dentistry, Osaka University, Osaka University, 565-0871 Osaka, Japan.
    Autophagy is a bulk protein-degradation process that is regulated by many factors. In this study, we quantitatively assessed the contribution of each essential yeast gene to autophagy. Of the contributing factors that we identified, we focused on the TRAPPIII complex, which was recently shown to act as a guanine-nucleotide exchange factor for the Rab small GTPase Ypt1. Read More