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Eukaryon

Class Year

2010

Abstract

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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Eukaryon is published by students at Lake Forest College, who are solely responsible for its content. The views expressed in Eukaryon do not necessarily reflect those of the College. Articles published within Eukaryon should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.

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