title: Biological roles of prion domains.
abstract: In vivo amyloid formation is a widespread phenomenon in eukaryotes. Self-perpetuating amyloids provide a basis for the infectious or heritable protein isoforms (prions). At least for some proteins, amyloid-forming potential is conserved in evolution despite divergence of the amino acid (aa) sequences. In some cases, prion formation certainly represents a pathological process leading to a disease. However, there are several scenarios in which prions and other amyloids or amyloid-like aggregates are either shown or suspected to perform positive biological functions. Proven examples include self/nonself recognition, stress defense and scaffolding of other (functional) polymers. The role of prion-like phenomena in memory has been hypothesized. As an additional mechanism of heritable change, prion formation may in principle contribute to heritable variability at the population level. Moreover, it is possible that amyloid-based prions represent by-products of the transient feedback regulatory circuits, as normal cellular function of at least some prion proteins is decreased in the prion state.
authors.affiliation: Department of Genetics, St. Petersburg State University, St. Petersburg, Russia.
authors.forename: Sergey G
authors.initials: SG
authors.lastname: Inge-Vechtomov
authors.forename: Galina A
authors.initials: GA
authors.lastname: Zhouravleva
authors.forename: Yury O
authors.initials: YO
authors.lastname: Chernoff
mesh_terms: D000595:Amino Acid Sequence / Q000235:genetics; D000682:Amyloid / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D006801:Humans; D008568:Memory; D011328:Prions / Q000235:genetics / Q000378:metabolism*; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000235:genetics
chemical_list: D000682:Amyloid; D011328:Prions; D020033:Protein Isoforms