The Natural History of Yeast Prions

Tuite, Mick F.

doi:10.1016/b978-0-12-407673-0.00003-5

Cited by 11 publications

(11 citation statements)

References 214 publications

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“…Although we focus this review on disease mechanisms, the discovery that prion-like processes govern heritable traits in certain fungi opened a rich and productive field of research that has yielded invaluable insights into the biology of prions (Krauss & Vorberg 2013, Liebman & Chernoff 2012, Newby & Lindquist 2013, Prusiner 2013, Sugiyama & Tanaka 2014, Tuite 2013, Wickner et al 2013). Prion-like processes also appear to influence functional protein aggregation in such phenomena as memory formation (Raveendra et al 2013, Si et al 2003), peptide storage (Maji et al 2009), and the innate immune response (Cai et al 2014, Hou et al 2011) and inflammation (Franklin et al 2014).…”

Section: Prion-like Processes Beyond the Nervous Systemmentioning

confidence: 99%

Neurodegenerative Diseases: Expanding the Prion Concept

Walker

Jucker

2015

Annu. Rev. Neurosci.

308

243

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The prion paradigm has emerged as a unifying molecular principle for the pathogenesis of many age-related neurodegenerative diseases. This paradigm holds that a fundamental cause of specific disorders is the misfolding and seeded aggregation of certain proteins. The concept arose from the discovery that devastating brain diseases called spongiform encephalopathies are transmissible to new hosts by agents consisting solely of a misfolded protein, now known as the prion protein. Accordingly, “prion” was defined as a “proteinaceous infectious particle.” As the concept has expanded to include other diseases, many of which are not infectious by any conventional definition, the designation of prions as infectious agents has become problematic. We propose to define prions as “proteinaceous nucleating particles” to highlight the molecular action of the agents, lessen unwarranted apprehension about the transmissibility of noninfectious proteopathies, and promote the wider acceptance of this revolutionary paradigm by the biomedical community.

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Section: Prion-like Processes Beyond the Nervous Systemmentioning

confidence: 99%

Neurodegenerative Diseases: Expanding the Prion Concept

Walker

Jucker

2015

Annu. Rev. Neurosci.

308

243

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“…Yeast prion proteins usually contain glutamine (Q) and asparagine (N) - rich prion domains (PrDs) responsible for prion propagation (Tuite, 2013). Polymerization of a prion-forming protein, resulting in formation of the initial prion “seed”, could be accelerated when the misfolded protein is present at a high local concentration.…”

Section: Introductionmentioning

confidence: 99%

“…Such prion induction is significantly enhanced by the presence of other QN-rich prions, or by simultaneous overproduction of other yeast proteins with QN-rich domains (Derkatch et al, 2001; Osherovich and Weissman, 2001). Some of these heterologous Q/N-rich inducers are known to form prions themselves, although such evidence is lacking for others (Alberti et al, 2009; Tuite, 2013). Functional interaction between PrDs of two yeast proteins, Pub1/TIA and Sup35 (Li et al, 2014), as well as promotion of polyglutamine aggregation by endogenous yeast prions (Gokhale et al, 2005; Meriin et al, 2002) suggest that Q/N-rich proteins can be co-assembled in cellular locations that become prion nucleation sites.…”

Section: Introductionmentioning

confidence: 99%

Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress

et al. 2017

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SUMMARY Self-perpetuating ordered protein aggregates (amyloids and prions) are associated with a variety of neurodegenerative disorders. Although environmental agents have been linked to certain amyloid diseases, the molecular basis of their action remains unclear. We have employed endogenous yeast prions as a model system to study environmental control of amyloid formation. A short-lived actin-associated yeast protein Lsb2 can trigger prion formation by other proteins in a mode regulated by the cytoskeleton and ubiquitin dependent processes. Here we show that that such a heterologous prion induction is due to the ability of Lsb2 to form a transient prion state, generated in response to thermal stress. Evolutionary acquisition of prion-inducing activity by Lsb2 is traced to a single amino acid change, coinciding with the acquisition of thermotolerance in the Saccharomyces yeast lineage. This raises the intriguing possibility that the transient prion formation could aid in functioning of Lsb2 at higher temperatures.

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“…Although a number of studies have shed light on how prions modify transcription of yeast (Holmes et al, 2013; True et al, 2004), the impact on transcriptional regulation by prion remains to be fully understood. Comparing to gene mutations, prion-mediated regulation has the advantage of not only being heritable but also reversible, as well as responsive to extreme environmental changes (Halfmann and Lindquist, 2010; Tuite, 2013). In particular, prion conformational switch of a global transcriptional regulator like Swi1 or Cyc8 may robustly alter the yeast transcriptome by turning on or off the expression of many target genes simultaneously (Du et al, 2008; Patel et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

The Yeast Prion [SWI+] Abolishes Multicellular Growth by Triggering Conformational Changes of Multiple Regulators Required for Flocculin Gene Expression

Zhang

2015

Cell Reports

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Summary While transcription factors are prevalent among yeast prion proteins, the role of prion-mediated transcriptional regulation remains elusive. We show here that the yeast prion [SWI+] abolishes flocculin (FLO) gene expression and results in a complete loss of multicellularity. Further investigation demonstrates that besides Swi1, multiple other proteins essential for FLO expression, including Mss11, Sap30, and Msn1 also undergo conformational changes, and become inactivated in [SWI+] cells. Moreover, the asparagine-rich region of Mss11 can exist as prion-like aggregates specifically in [SWI+] cells, which are SDS-resistant, heritable, and curable, but become metastable after separation from [SWI+]. Our findings thus reveal a prion-mediated mechanism through which multiple regulators in a biological pathway can be inactivated. In combination with the partial loss-of-function phenotypes of [SWI+] cells on non-glucose sugar utilization, our data therefore demonstrate that a prion can influence differently on distinct traits through multi-level regulations, providing insights into the biological roles of prions.

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The Natural History of Yeast Prions

Cited by 11 publications

References 214 publications

Neurodegenerative Diseases: Expanding the Prion Concept

Neurodegenerative Diseases: Expanding the Prion Concept

Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress

The Yeast Prion [SWI+] Abolishes Multicellular Growth by Triggering Conformational Changes of Multiple Regulators Required for Flocculin Gene Expression

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