| START Conference Manager |
Parkinson’s disease (PD) has been linked to impaired recycling and accumulation of the misfolded protein, α-synuclein. Therefore, increasing degradation of α-synuclein is of therapeutic interest. A current hypothesis explains that endocytosis at the lysosome is one of the routes to α-synuclein degradation. Previously, our lab found genetic evidence that endocytosis pathway complexes (pre-ESCRT, ESCRT-I, ESCRT-II, ESCRT-III and post-ESCRT) regulate several α–synuclein PD related properties. Most importantly, our lab found that the vascular sorting protein vps28 (a ESCRT-I gene) altered α-synuclein localization and increased its accumulation and toxicity in a yeast PD model. To extend this work, I investigated if increasing the concentration of α-synuclein in yeast that lack vps28 further increased α-synuclein accumulation and toxicity and I found that it did. Together, these studies illustrate the growing relevance of endocytosis in PD pathology.
[Abstract (DOC)]