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Prion. 2016 May 3;10(3):182-206. doi: 10.1080/19336896.2016.1181253.

Prions, amyloids, and RNA: Pieces of a puzzle.

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a Dept. of Genetics and Biotechnology , St. Petersburg State University , St. Petersburg , Russia.
b Vavilov Institute of General Genetics of the Russian Academy of Sciences, St. Petersburg Branch , St. Petersburg , Russia.
c All-Russia Research Institute for Agricultural Microbiology , St. Petersburg , Russia.
d Department of Neuroscience , College of Physicians and Surgeons of Columbia University, Columbia University , New York , NY , USA.


Amyloids are protein aggregates consisting of fibrils rich in β-sheets. Growth of amyloid fibrils occurs by the addition of protein molecules to the tip of an aggregate with a concurrent change of a conformation. Thus, amyloids are self-propagating protein conformations. In certain cases these conformations are transmissible / infectious; they are known as prions. Initially, amyloids were discovered as pathological extracellular deposits occurring in different tissues and organs. To date, amyloids and prions have been associated with over 30 incurable diseases in humans and animals. However, a number of recent studies demonstrate that amyloids are also functionally involved in a variety of biological processes, from biofilm formation by bacteria, to long-term memory in animals. Interestingly, amyloid-forming proteins are highly overrepresented among cellular factors engaged in all stages of mRNA life cycle: from transcription and translation, to storage and degradation. Here we review rapidly accumulating data on functional and pathogenic amyloids associated with mRNA processing, and discuss possible significance of prion and amyloid networks in the modulation of key cellular functions.


Amyloid; CPEB; Prion; Pub1; S. cerevisiae; Sup35; Tia1; yeast

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