Parkinson's Disease, α-synuclein degradation
Misfolding and toxic accumulation of α-synuclein is thought to cause Parkinson’s disease. Developing ways to reduce a-Synuclein accumulation may lead to future treatments. The dominant model of α-synuclein degradation is by the proteasome degradation pathway where α-synuclein toxicity has been associated with malfunctions in this pathway. However, evidence is building to suggest that the multivesicular body (MVB) sorting pathway to degradation via the vacuole/ lysosome also degrades α-synuclein and that malfunctions in this pathway lead to α-synuclein accumulation and toxicity. Here we demonstrate that the absence of vps28, an essential component of the MVB sorting pathway, increases the toxicity of both wild type and mutant forms of α-synuclein. The absence of vps28 also significantly alters the cellular distribution and localization of α-synuclein and increases its cytoplasmic aggregation. We propose that dysfunction of the MVB sorting pathway to the vacuole/lysosome can lead to the pathology linked to Parkinson’s disease, including cell death.
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.