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Parkinson’s disease (PD) is an incurable neurodegenerative disorder linked to the accumulation, misfolding, and aggregation of the α-synuclein protein in midbrain dopaminergic neurons. Enhancing α-synuclein degradation may be an effective goal for future drugs. Strong evidence links the proteasome and lysosome as degradation sites for α-synuclein. Recently, α-synuclein was found associated with plasma membranes and outside of cells, suggesting that α-synuclein might use the MVB/endocytosis pathway as a route to the lysosome. We tested this hypothesis in a S. cerevisiae model for PD. In yeast gene deletion strains lacking vps34 or vps27 (both involved in the initial pre-ESCRT step in this pathway), we assessed if α-synuclein accumulated, changed cellular localization, and induced toxicity. We report three significant findings. Firstly, α-synuclein altered its cellular localization in both deletion strains. Secondly, α-synuclein accumulated in vps34Δ cells. Lastly, the absence of either gene had no effect on toxicity. Together, our results suggest that the pre-ESCRT step in the MVB/endosome pathway is involved in degrading α-synuclein, although in an unexpectedly complex way.

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