α-Synuclein fate: proteasome or autophagy?

Autophagy
Simone Engelender

Abstract

The accumulation of α-synuclein is critical for the development of Parkinson disease (PD), and unraveling the mechanisms that regulate α-synuclein levels is key to understanding the pathophysiology of the disease. We recently found that USP9X deubiquitinates α-synuclein, and that this process determines the partition of α-synuclein between the proteasomal and autophagy pathways. By manipulating USP9X levels, we observed that monoubiquitinated α-synuclein is degraded by the proteasome, whereas deubiquitination of α-synuclein favors its degradation by autophagy. As USP9X levels and activity are decreased in α-synucleinopathy brains, USP9X may now represent a novel target for PD.

Citations

Jan 23, 2013·Molecular Neurobiology·Laura CampelloJosé Martín-Nieto
Apr 23, 2013·Acta Pharmacologica Sinica·Fang YangChun-feng Liu
Jan 5, 2014·Molecular Neurobiology·Deepak ChhanganiAmit Mishra
Sep 11, 2014·International Journal of Molecular Sciences·Guobin LiPeng Lun
Jan 19, 2016·Frontiers in Cellular Neuroscience·Bruno Di Marco VieiraDean L Pountney
Sep 15, 2014·Journal of Neural Transmission·Filippo Sean GiorgiFrancesco Fornai
Feb 13, 2015·Cellular and Molecular Life Sciences : CMLS·Mariyam MurtazaStephen A Wood
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Jun 3, 2015·Molecular and Cellular Biology·Yi-Sheng HouZheng-Hong Qin
May 22, 2019·Acta Neuropathologica Communications·Zuzana KrejciovaStanley B Prusiner
Aug 30, 2020·Neural Regeneration Research·Claudio GiulianoFabio Blandini
Jan 17, 2019·Oxidative Medicine and Cellular Longevity·Gloria LazzeriFrancesco Fornai
Apr 30, 2020·International Journal of Molecular Sciences·Fiona LimanaqiFrancesco Fornai

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