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Eukaryon

Class Year

2010

Abstract

Parkinson's disease (PD) is a neurodegenerative disorder linked to the accumulation, misfolding, and aggregation of the alpha-synuclein protein in dopaminergic neurons of the midbrain, which might ultimately lead to the death of these neurons. Until recently, the proteasome was believed to be the main pathway for alpha-synuclein degradation; however, strong evidence emerged that supports the lysosome as another mechanism that effectively degrades the protein. The two pathways to the lysosome are autophagy and endocytosis. More evidence for autophagy as a mechanism for alpha-synuclein degradation is available, even though some studies point to the MVB/endocytosis pathway a route for membrane bound and extra cellular protein degradation. I propose the hypothesis that the MVB/endocytosis pathway is a route through which alpha-synuclein is targeted to the lysosome. Using S. cerevisiae as a model system, I will assess if alpha-synuclein accumulates, changes localization, and induces cell toxicity in yeasts genetically compromised for endocytosis at the pre-ESCRT step: vps27 and vps34. The pre-ESCRT gene knockouts will be compared with intact endocytosis intact yeast strains, while also comparing a-synuclein containing vectors to alpha-synuclein absent vectors. With around four million people affected worldwide, finding a cure for PD is a worldwide concern and priority.

bio324-proposal-perez.ppt (3936 kB)
Supplemental PowerPoint file

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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