| Literature DB >> 26940507 |
Louise Berkhoudt Lassen1, Lasse Reimer1, Nelson Ferreira1, Cristine Betzer1, Poul Henning Jensen1.
Abstract
α-synuclein is normally situated in the nerve terminal but it accumulates and aggregates in axons and cell bodies in synucleinopathies such as Parkinson's disease. The conformational changes occurring during α-synucleins aggregation process affects its interactions with other proteins and its subcellular localization. This review focuses on interaction partners of α-synuclein within different compartments of the cell with a focus on those preferentially binding aggregated α-synuclein. The aggregation state of α-synuclein also affects its catabolism and we hypothesize impaired macroautophagy is involved neuronal excretion of α-synuclein species responsible for the prion-like spreading of α-synuclein pathology.Entities:
Keywords: Lewy Body; Parkinson's disease; dementia; neurodegeneration; protein interaction; proteomics; α-synuclein
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Year: 2016 PMID: 26940507 DOI: 10.1111/bpa.12374
Source DB: PubMed Journal: Brain Pathol ISSN: 1015-6305 Impact factor: 6.508