Open AccessProtein Partners of α‐Synuclein in Health and Disease
Author(s) -
Lassen Louise Berkhoudt,
Reimer Lasse,
Ferreira Nelson,
Betzer Cristine,
Jensen Poul Henning
Publication year - 2016
Publication title -
brain pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.986
H-Index - 132
eISSN - 1750-3639
pISSN - 1015-6305
DOI - 10.1111/bpa.12374
Subject(s) - synucleinopathies , alpha synuclein , neuroscience , microbiology and biotechnology , biology , protein aggregation , lewy body , disease , cell , protein folding , parkinson's disease , synuclein , chemistry , pathology , medicine , biochemistry
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.