Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip.
Amyloid
/ chemistry
Amyloidogenic Proteins
/ chemistry
Animals
Autophagy
Disease Resistance
/ immunology
Disease Susceptibility
/ immunology
Fungal Proteins
/ chemistry
Host-Pathogen Interactions
/ genetics
Humans
Immunity, Innate
Molecular Chaperones
/ metabolism
Mutation
Nonsense Mediated mRNA Decay
Prion Diseases
/ etiology
Prions
/ chemistry
Protein Binding
Protein Conformation
Protein Folding
Ribosomes
/ metabolism
Anti-prion system
Btn2
Hsp104
Prion
Ribosome-associated chaperones
Upf1
Journal
Current genetics
ISSN: 1432-0983
Titre abrégé: Curr Genet
Pays: United States
ID NLM: 8004904
Informations de publication
Date de publication:
Dec 2021
Dec 2021
Historique:
received:
07
06
2021
accepted:
07
07
2021
revised:
06
07
2021
pubmed:
29
7
2021
medline:
24
2
2022
entrez:
28
7
2021
Statut:
ppublish
Résumé
The yeast prions (infectious proteins) [URE3] and [PSI+] are essentially non-functional (or even toxic) amyloid forms of Ure2p and Sup35p, whose normal function is in nitrogen catabolite repression and translation termination, respectively. Yeast has an array of systems working in normal cells that largely block infection with prions, block most prion formation, cure most nascent prions and mitigate the toxic effects of those prions that escape the first three types of systems. Here we review recent progress in defining these anti-prion systems, how they work and how they are regulated. Polymorphisms of the prion domains partially block infection with prions. Ribosome-associated chaperones ensure proper folding of nascent proteins, thus reducing [PSI+] prion formation and curing many [PSI+] variants that do form. Btn2p is a sequestering protein which gathers [URE3] amyloid filaments to one place in the cells so that the prion is often lost by progeny cells. Proteasome impairment produces massive overexpression of Btn2p and paralog Cur1p, resulting in [URE3] curing. Inversely, increased proteasome activity, by derepression of proteasome component gene transcription or by 60S ribosomal subunit gene mutation, prevents prion curing by Btn2p or Cur1p. The nonsense-mediated decay proteins (Upf1,2,3) cure many nascent [PSI+] variants by associating with Sup35p directly. Normal levels of the disaggregating chaperone Hsp104 can also cure many [PSI+] prion variants. By keeping the cellular levels of certain inositol polyphosphates / pyrophosphates low, Siw14p cures certain [PSI+] variants. It is hoped that exploration of the yeast innate immunity to prions will lead to discovery of similar systems in humans.
Identifiants
pubmed: 34319422
doi: 10.1007/s00294-021-01203-1
pii: 10.1007/s00294-021-01203-1
doi:
Substances chimiques
Amyloid
0
Amyloidogenic Proteins
0
Fungal Proteins
0
Molecular Chaperones
0
Prions
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
833-847Informations de copyright
© 2021. This is a U.S. government work and not under copyright protection in the U.S.; foreign copyright protection may apply.
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