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Eukaryon

Class Year

2009

Abstract

Parkinson’s disease is a fatal and incurable human neurodegenerative disorder that destroys midbrain neurons. The misfolding, accumulation, and aggregation of the protein alpha-synuclein is thought to kill these cells. Enhancing alpha-synuclein degradation may help prevent its accumulation and aggregation, while protecting cells against toxicity. For this thesis, we used the model organism budding yeast to evaluate the hypothesis that alpha-synuclein is degraded by the cellular organelle lysosome via a specific route: the MVB/endocytosis pathway. Specifically, we evaluated whether three disease-related properties of alpha-synuclein (aggregation, accumulation, and toxicity) worsened in yeast strains that were individually deleted for genes coding for proteins required for the MVB/endocytosis pathway. In support of our hypothesis, each gene deletion altered one or more alpha-synuclein properties. While our data indicates that the MVB pathway is a route for alpha-synuclein degradation, the specificity and extent of alpha-synuclein involvement with proteins within the ESCRT complexes appears unexpectedly complex.

Disclaimer

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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