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Differential Interactions of Molecular Chaperones and Yeast Prions
Baker’s yeast Saccharomyces cerevisiae is an important model organism that is applied to study various aspects of eukaryotic cell biology. Prions in yeast are self-perpetuating heritable protein aggregates that can be leveraged to study the interaction between the protein quality control (PQC) machi...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8877571/ https://www.ncbi.nlm.nih.gov/pubmed/35205876 http://dx.doi.org/10.3390/jof8020122 |
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author | Barbitoff, Yury A. Matveenko, Andrew G. Zhouravleva, Galina A. |
author_facet | Barbitoff, Yury A. Matveenko, Andrew G. Zhouravleva, Galina A. |
author_sort | Barbitoff, Yury A. |
collection | PubMed |
description | Baker’s yeast Saccharomyces cerevisiae is an important model organism that is applied to study various aspects of eukaryotic cell biology. Prions in yeast are self-perpetuating heritable protein aggregates that can be leveraged to study the interaction between the protein quality control (PQC) machinery and misfolded proteins. More than ten prions have been identified in yeast, of which the most studied ones include [PSI(+)], [URE3], and [PIN(+)]. While all of the major molecular chaperones have been implicated in propagation of yeast prions, many of these chaperones differentially impact propagation of different prions and/or prion variants. In this review, we summarize the current understanding of the life cycle of yeast prions and systematically review the effects of different chaperone proteins on their propagation. Our analysis clearly shows that Hsp40 proteins play a central role in prion propagation by determining the fate of prion seeds and other amyloids. Moreover, direct prion-chaperone interaction seems to be critically important for proper recruitment of all PQC components to the aggregate. Recent results also suggest that the cell asymmetry apparatus, cytoskeleton, and cell signaling all contribute to the complex network of prion interaction with the yeast cell. |
format | Online Article Text |
id | pubmed-8877571 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-88775712022-02-26 Differential Interactions of Molecular Chaperones and Yeast Prions Barbitoff, Yury A. Matveenko, Andrew G. Zhouravleva, Galina A. J Fungi (Basel) Review Baker’s yeast Saccharomyces cerevisiae is an important model organism that is applied to study various aspects of eukaryotic cell biology. Prions in yeast are self-perpetuating heritable protein aggregates that can be leveraged to study the interaction between the protein quality control (PQC) machinery and misfolded proteins. More than ten prions have been identified in yeast, of which the most studied ones include [PSI(+)], [URE3], and [PIN(+)]. While all of the major molecular chaperones have been implicated in propagation of yeast prions, many of these chaperones differentially impact propagation of different prions and/or prion variants. In this review, we summarize the current understanding of the life cycle of yeast prions and systematically review the effects of different chaperone proteins on their propagation. Our analysis clearly shows that Hsp40 proteins play a central role in prion propagation by determining the fate of prion seeds and other amyloids. Moreover, direct prion-chaperone interaction seems to be critically important for proper recruitment of all PQC components to the aggregate. Recent results also suggest that the cell asymmetry apparatus, cytoskeleton, and cell signaling all contribute to the complex network of prion interaction with the yeast cell. MDPI 2022-01-27 /pmc/articles/PMC8877571/ /pubmed/35205876 http://dx.doi.org/10.3390/jof8020122 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Barbitoff, Yury A. Matveenko, Andrew G. Zhouravleva, Galina A. Differential Interactions of Molecular Chaperones and Yeast Prions |
title | Differential Interactions of Molecular Chaperones and Yeast Prions |
title_full | Differential Interactions of Molecular Chaperones and Yeast Prions |
title_fullStr | Differential Interactions of Molecular Chaperones and Yeast Prions |
title_full_unstemmed | Differential Interactions of Molecular Chaperones and Yeast Prions |
title_short | Differential Interactions of Molecular Chaperones and Yeast Prions |
title_sort | differential interactions of molecular chaperones and yeast prions |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8877571/ https://www.ncbi.nlm.nih.gov/pubmed/35205876 http://dx.doi.org/10.3390/jof8020122 |
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