Abstract
Protein misfolding is associated with many neurodegenerative diseases, including neurodegenerative diseases caused by polyglutamine expansion proteins, such as Huntington’s disease. The model organism baker’s yeast (Saccharomyces cerevisiae) has provided important general insights into the basic cellular mechanisms underlying protein misfolding. Furthermore, experiments in yeast have identified cellular factors that modulate the toxicity and the aggregation associated with polyglutamine expansion proteins. Notably, many features discovered in yeast have been proven to be highly relevant in other model organisms and in human pathology. The experimental protocols depicted here serve to reliably determine polyglutamine toxicity and polyglutamine aggregation in yeast.
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Acknowledgments
Research in the Duennwald lab is supported by grants from the American Federation for Aging Research (AFAR), the Hereditary Disease Foundation (HDF), and the William Wood Foundation.
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Duennwald, M.L. (2013). Yeast as a Platform to Explore Polyglutamine Toxicity and Aggregation. In: Hatters, D., Hannan, A. (eds) Tandem Repeats in Genes, Proteins, and Disease. Methods in Molecular Biology, vol 1017. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-438-8_11
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DOI: https://doi.org/10.1007/978-1-62703-438-8_11
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