Differential Interactions of Molecular Chaperones and Yeast Prions

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Differential Interactions of Molecular Chaperones and Yeast Prions. / Barbitoff, Yury A.; Matveenko, Andrew G.; Zhouravleva, Galina A.

In: Journal of Fungi, Vol. 8, No. 2, 122, 02.2022.

Research output: Contribution to journal › Review article › peer-review

BibTeX

@article{e174854173de408faaae2bbff7443d35,

title = "Differential Interactions of Molecular Chaperones and Yeast Prions",

abstract = "Baker{\textquoteright}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.",

keywords = "Chaperone, Hsp104, Prion propagation, Protein quality control, Sis1, Yeast prion",

author = "Barbitoff, {Yury A.} and Matveenko, {Andrew G.} and Zhouravleva, {Galina A.}",

note = "Publisher Copyright: {\textcopyright} 2022 by the authors. Licensee MDPI, Basel, Switzerland.",

year = "2022",

month = feb,

doi = "10.3390/jof8020122",

language = "English",

volume = "8",

journal = "Journal of Fungi",

issn = "2309-608X",

publisher = "MDPI AG",

number = "2",

}

RIS

TY - JOUR

T1 - Differential Interactions of Molecular Chaperones and Yeast Prions

AU - Barbitoff, Yury A.

AU - Matveenko, Andrew G.

AU - Zhouravleva, Galina A.

PY - 2022/2

Y1 - 2022/2

N2 - 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.

AB - 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.

KW - Chaperone

KW - Hsp104

KW - Prion propagation

KW - Protein quality control

KW - Sis1

KW - Yeast prion

UR - http://www.scopus.com/inward/record.url?scp=85123775579&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/961e2c45-ea74-3a72-9843-490c8b396d1e/

U2 - 10.3390/jof8020122

DO - 10.3390/jof8020122

M3 - Review article

C2 - 35205876

AN - SCOPUS:85123775579

VL - 8

JO - Journal of Fungi

JF - Journal of Fungi

SN - 2309-608X

IS - 2

M1 - 122

ER -

ID: 96582173