TY - JOUR

T1 - Biological roles of prion domains.

AU - Inge-Vechtomov, Sergey G.

AU - Zhouravleva, Galina A.

AU - Chernoff, Yury O.

N1 - Funding Information: We thank R.B. Wickner and G.P. Newnam for critical reading of the manuscript and helpful suggestions. This work was supported by grants ST-012 from CRDF, RAS Presidium Program “Biosphere origin and evolution” and (Lot 2006-12.2/001) from Federal Agency of Science and Innovations (to Sergey G. Inge-Vechtomov and Galina A. Zhouravleva), by grant 07-04-00605 from the Russian Foundation for Basic Research (to Galina A. Zhouravleva), and by grant R01GM58763 from NIH (to Yury O. Chernoff ). Copyright: This record is sourced from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

PY - 2007/10

Y1 - 2007/10

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=51049106982&partnerID=8YFLogxK

U2 - 10.4161/pri.1.4.5059

DO - 10.4161/pri.1.4.5059

M3 - Review article

C2 - 19172114

AN - SCOPUS:51049106982

VL - 1

SP - 228

EP - 235

JO - Prion

JF - Prion

SN - 1933-6896

IS - 4

ER -