ArticleMolecular microbiology2015
Feedback control of prion formation and propagation by the ribosome-associated chaperone complex.
Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
36 citing papers in PubMed, 42 citations in OpenAlex.
- Detection system- and strain-dependent diversity of de novo [PSI+] prion generation and phenotypes in Saccharomyces cerevisiae.Journal of microbiology (Seoul, Korea) · 2025Article
- Yeast Prions: Discovery, Nature, Cellular Manipulation and Implication.Journal of microbiology and biotechnology · 2025Review
- Total propagation of yeast prion conformers in ssz1∆ upf1∆ Hsp104Current genetics · 2025Article
- Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025Review
- Human proteins curing yeast prions.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Prions in Microbes: The Least in the Most.Journal of microbiology (Seoul, Korea) · 2023Review
- Article
- Yeast Chaperone Hsp70-Ssb Modulates a Variety of Protein-Based Heritable Elements.International journal of molecular sciences · 2023Article
- Prions are the greatest protein misfolding problem, and yeast has several solutions.PLoS pathogens · 2023Article
- Anti-Prion Systems inViruses · 2022Review
- Review
- Antiprion systems in yeast cooperate to cure or prevent the generation of nearly all [Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022Review
- Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip.Current genetics · 2021Review
- Regulation of the endocytosis and prion-chaperoning machineries by yeast E3 ubiquitin ligase Rsp5 as revealed by orthogonal ubiquitin transfer.Cell chemical biology · 2021Article
- Proteasome Control of [URE3] Prion Propagation by Degradation of Anti-Prion Proteins Cur1 and Btn2 in Saccharomyces cerevisiae.Genetics · 2021Article
- Normal levels of ribosome-associated chaperones cure two groups of [PSI+] prion variants.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020Review
- Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery.Molecules (Basel, Switzerland) · 2019Review
- Role of the Cell Asymmetry Apparatus and Ribosome-Associated Chaperones in the Destabilization of aGenetics · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
Cross-beta fibrous protein aggregates (amyloids and amyloid-based prions) are found in mammals (including humans) and fungi (including yeast), and are associated with both diseases and heritable traits. The Hsp104/70/40 chaperone machinery controls propagation of yeast prions. The Hsp70 chaperones Ssa and Ssb show opposite effects on [PSI(+)], a prion form of the translation termination factor Sup35 (eRF3). Ssb is bound to translating ribosomes via ribosome-associated complex (RAC), composed of Hsp40-Zuo1 and Hsp70-Ssz1. Here we demonstrate that RAC disruption increases de novo prion formation in a manner similar to Ssb depletion, but interferes with prion propagation in a manner similar to Ssb overproduction. Release of Ssb into the cytosol in RAC-deficient cells antagonizes binding of Ssa to amyloids. Thus, propagation of an amyloid formed because of lack of ribosome-associated Ssb can be counteracted by cytosolic Ssb, generating a feedback regulatory circuit. Release of Ssb from ribosomes is also observed in wild-type cells during growth in poor synthetic medium. Ssb is, in a significant part, responsible for the prion destabilization in these conditions, underlining the physiological relevance of the Ssb-based regulatory circuit.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.