Title: P2–034: Deletion of genes responsible for vesicular transport in yeast causes mislocalization and enhanced toxicity of α–synuclein
Abstract:α–Synuclein is a small pre–synaptic protein involved in the pathology of Parkinson. The function of α–synuclein is still unclear but was recently suggested to be important for vesicular transport. In ...α–Synuclein is a small pre–synaptic protein involved in the pathology of Parkinson. The function of α–synuclein is still unclear but was recently suggested to be important for vesicular transport. In order to define a role of α–synuclein in vesicular transport and vesicular pathways, we expressed α–synuclein as a native or as a GFP–tagged fusion protein in the yeast Saccharomyces cerevisiae. This is a suitable model since yeast expresses many functional orthologues of mammalian vesicular proteins. Similar to its localization in mammalian cells, both native α–synuclein and α–synuclein–GFP were bound to the cytoplasmic side of the plasma membrane in wild type yeast cells (Zabrocki et al., FEBS J., 272, 1386–1400, 2005). We screened mutant yeast strains lacking different proteins that are proven or suspected to be involved in vesicular transport. We observed distinct patterns of α–synuclein mislocalization, that often coincided with enhanced toxicity of α–synuclein. We provide evidence for connections of α–synuclein to vesicular transport involving ESCRT I, II, III complexes, SNAREs, the HOPS complex and typical proteins of the Golgi complex. Many of these proteins are related to endosomal and ubiquitin–dependent transport, which links α–synuclein to different vesicular transport systems.Read More
Publication Year: 2006
Publication Date: 2006-07-01
Language: en
Type: article
Indexed In: ['crossref']
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