Journal
JOVE-JOURNAL OF VISUALIZED EXPERIMENTS
Volume -, Issue 95, Pages -Publisher
JOURNAL OF VISUALIZED EXPERIMENTS
DOI: 10.3791/52321
Keywords
Cellular Biology; Issue 95; Caenorhabditis elegans; neurodegenerative diseases; protein misfolding diseases; prion-like spreading; cell-to-cell transmission; protein aggregation; non-cell autonomous toxicity; proteostasis
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Funding
- National Institutes of Health (NIGMS)
- National Institutes of Health (NIA)
- National Institutes of Health (NINDS)
- Ellison Medical Foundation
- Daniel F. and Ada L. Rice Foundation
- Deutsche Forschungsgemeinschaft [KR 3726/1-1]
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Prions are unconventional self-propagating proteinaceous particles, devoid of any coding nucleic acid. These proteinaceous seeds serve as templates for the conversion and replication of their benign cellular isoform. Accumulating evidence suggests that many protein aggregates can act as self-propagating templates and corrupt the folding of cognate proteins. Although aggregates can be functional under certain circumstances, this process often leads to the disruption of the cellular protein homeostasis (proteostasis), eventually leading to devastating diseases such as Alzheimer's disease (AD), Parkinson's disease (PD), Amyotrophic lateral sclerosis (ALS), or transmissible spongiform encephalopathies (TSEs). The exact mechanisms of prion propagation and cell-to-cell spreading of protein aggregates are still subjects of intense investigation. To further this knowledge, recently a new metazoan model in Caenorhabditis elegans, for expression of the prion domain of the cytosolic yeast prion protein Sup35 has been established. This prion model offers several advantages, as it allows direct monitoring of the fluorescently tagged prion domain in living animals and ease of genetic approaches. Described here are methods to study prion-like behavior of protein aggregates and to identify modifiers of prion-induced toxicity using C. elegans.
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