2023
DOI: 10.3390/ijms241411651
|View full text |Cite
|
Sign up to set email alerts
|

How Big Is the Yeast Prion Universe?

Abstract: The number of yeast prions and prion-like proteins described since 1994 has grown from two to nearly twenty. If in the early years most scientists working with the classic mammalian prion, PrPSc, were skeptical about the possibility of using the term prion to refer to yeast cytoplasmic elements with unusual properties, it is now clear that prion-like phenomena are widespread and that yeast can serve as a convenient model for studying them. Here we give a brief overview of the yeast prions discovered so far and… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1

Citation Types

0
3
0

Year Published

2024
2024
2024
2024

Publication Types

Select...
2

Relationship

1
1

Authors

Journals

citations
Cited by 2 publications
(3 citation statements)
references
References 116 publications
0
3
0
Order By: Relevance
“…Primarily, this is because they are prone to either amyloid aggregation or phase separation-based inclusion formation (or both); a number of instances in which they may aid in aggregation of each other have been documented [10,13,54]. Among the Q/N-rich proteins, transcription regulators are frequently found (reviewed in [15]). Several attempts ta screening for such factors affecting the [PSI + ] prion or nonsense suppression have been made; however, these have yielded contradictory results.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Primarily, this is because they are prone to either amyloid aggregation or phase separation-based inclusion formation (or both); a number of instances in which they may aid in aggregation of each other have been documented [10,13,54]. Among the Q/N-rich proteins, transcription regulators are frequently found (reviewed in [15]). Several attempts ta screening for such factors affecting the [PSI + ] prion or nonsense suppression have been made; however, these have yielded contradictory results.…”
Section: Discussionmentioning
confidence: 99%
“…These interactions are not limited to only prion-forming proteins; various other Q/N-rich proteins have been shown to act as Pin + -factors [10] as well as to form nonheritable aggregates [13,14] that can indirectly affect prion properties. Notably, transcription factors are often found among Q/N-rich proteins, with at least four of them forming bona fide prions: Ure2, Swi1, Mot3, and Cyc8 (reviewed in [14,15]).…”
Section: Introductionmentioning
confidence: 99%
“…Currently, about nine yeast amyloid prions are known [ 6 , 7 ]. Two of the best-studied yeast prions are the Sup35 protein, which phenotypically manifests as a nonsense-suppressor [ PSI +] determinant, and the Rnq1 protein, which manifests as a [ PIN +] determinant that greatly enhances the de novo appearance of [ PSI +] and other prions [ 8 ].…”
Section: Introductionmentioning
confidence: 99%