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Presentation Title

Creating tools to examine the contribution of C-terminal truncation variants of α-synuclein in Parkinson's Disease pathology

Location

Durand Art Institute, 2nd Floor Balcony

Abstract

Parkinson's disease (PD) is a hypokinetic neurodegenerative disorder characterized by the death of midbrain dopaminergic neurons. It is linked to the misfolding and aggregation of the protein α-synuclein that accumulates as Lewy bodies. The full-length α-synuclein (140 amino acids) was recently found in several carboxyl-terminal truncation variants (Lewis et al. 2010). While these variants can increase the aggregation and toxicity of the full-length α-synuclein in vitro (Li et al., 2005; Liu et al., 2005), the individual properties are not well-studied. We sought to test that these variants would reduce α-synuclein solubility, membrane association, and increase toxicity in organisms. We created four variants with GFP-tagged α-synuclein to study their properties in budding yeast (Saccharomyces cerevisiae).

Presentation Type

Poster

Start Date

4-8-2014 2:40 PM

End Date

4-8-2014 4:00 PM

Panel

Posters: The Ken Weik Poster Session

Field of Study for Presentation

Neuroscience

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Apr 8th, 2:40 PM Apr 8th, 4:00 PM

Creating tools to examine the contribution of C-terminal truncation variants of α-synuclein in Parkinson's Disease pathology

Durand Art Institute, 2nd Floor Balcony

Parkinson's disease (PD) is a hypokinetic neurodegenerative disorder characterized by the death of midbrain dopaminergic neurons. It is linked to the misfolding and aggregation of the protein α-synuclein that accumulates as Lewy bodies. The full-length α-synuclein (140 amino acids) was recently found in several carboxyl-terminal truncation variants (Lewis et al. 2010). While these variants can increase the aggregation and toxicity of the full-length α-synuclein in vitro (Li et al., 2005; Liu et al., 2005), the individual properties are not well-studied. We sought to test that these variants would reduce α-synuclein solubility, membrane association, and increase toxicity in organisms. We created four variants with GFP-tagged α-synuclein to study their properties in budding yeast (Saccharomyces cerevisiae).