Many neurodegenerative diseases are associated with accumulation of toxic, highly structured self-assembled protein aggregates, termed amyloids. Recently emerging evidence indicates that many amyloids possess transmissible (prion-like) properties. In yeast, endogenous prions transmit phenotypically detectable traits. Some amyloid-likeandprion-likeprotein polymers have been linked to biologically positive phenomena. In vitro experiments suggest that many proteins possess amyloidogenic properties. However, formation and propagation of amyloids are difficult to investigate in vivo due to complexity of the human organism. Therefore, we have established a yeast model for studying prion properties of mammalian proteins. We have demonstrated that fusion of a mammalian amyloidogenic protein to the prion domain of the yeast prion protein Sup35 enables such a chimeric construct to nucleate a prion in the absence of any pre-existing prions in the yeast cell. Phenotypic and biochemical detection assays, previously develop