Class Year



wildtype α-synuclein, optical density analysis, dilution series spotting, galactose media toxicity, cell lysates


α-Synuclein is implicated in Parkinson’s Disease, a neurodegenerative disease that destroys midbrain neurons. The misfolding and subsequent aggregation of this protein is the likely cause of cell death. A major hypothesis in the field is that increasing α-synuclein’s rate of degradation may prevent its aggregation and toxicity. The prevalent model for α-synuclein degradation is via the proteasome, and malfunctions in this pathway have been shown to increase α-synuclein accumulation and toxicity. However, increasing evidence suggests that the Multivesicular Body (MVB) sorting pathway is involved in protein degradation via the lysosome. To test the role of the MVB sorting pathway for the degradation of wild-type and mutant α-synucleins, we asked if α-synuclein would accumulate and increase toxicity in yeast that lacked one of the MVB proteins. Previously, Price and Shrestha showed that the absence of vps28, an MVB protein caused toxicity in yeast expressing α-synuclein (Eukaryon). We tested another protein, vps34, a PI 3-kinase acting upstream in the proteins involved in the MVB pathway. The absence of vps34 was toxic to yeast and this toxicity was severely exacerbated in the presence of any foreign protein, including α-synuclein. Future research will examine several other essential lysosomal pathway factors in mediating α-synuclein toxicity.


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