title: Differential Interactions of Molecular Chaperones and Yeast Prions
metadata.name: dc.contributor.author
metadata.value: Barbitoff, Yury A
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Matveenko, Andrew G
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Zhouravleva, Galina A
metadata.lang: -
metadata.name: dc.date.accessioned
metadata.value: 2022-06-14T20:18:21Z
metadata.lang: -
metadata.name: dc.date.available
metadata.value: 2022-06-14T20:18:21Z
metadata.lang: -
metadata.name: dc.date.issued
metadata.value: 2022-01-27
metadata.lang: -
metadata.name: dc.identifier
metadata.value: 10.3390/jof8020122
metadata.lang: -
metadata.name: dc.identifier.issn
metadata.value: 10.3390/jof8020122
metadata.lang: -
metadata.name: dc.identifier.uri
metadata.value: http://hdl.handle.net/11701/36679
metadata.lang: -
metadata.name: dc.description.abstract
metadata.value: 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.
metadata.lang: en_GB
metadata.name: dc.description.sponsorship
metadata.value: RSF grant 18-14-00050 (Part «Yeast prions and their life cycle») and the RFBR grant 19-04-00173 (other parts)
metadata.lang: en_GB
metadata.name: dc.language.iso
metadata.value: en
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: yeast prion
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: Sis1
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: chaperone
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: prion propagation
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: protein quality control
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: Hsp104
metadata.lang: en_GB
metadata.name: dc.title
metadata.value: Differential Interactions of Molecular Chaperones and Yeast Prions
metadata.lang: en_GB
metadata.name: dc.type
metadata.value: Article
metadata.lang: en_GB
resources.filename: 2022_Barbitoff et al._Differential Interactions of Molecular Chaperones and Yeast Prions.pdf
resources.url: https://dspace.spbu.ru/bitstream/11701/36679/1/2022_Barbitoff%20et%20al._Differential%20Interactions%20of%20Molecular%20Chaperones%20and%20Yeast%20Prions.pdf
resources.format: Adobe PDF
resources.size: 1,95 MB