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Accumulation of amyloid-like aggregates is a hallmark of numerous neurodegenerative disorders such as Alzheimer’s and polyglutamine disease. Yet, whether the amyloid inclusions found in these diseases are toxic or cytoprotective remains unclear. Various studies suggest that the toxic culprit in the amyloid …
Douglas Cyr, Philipp Trepte, Hong Yu Ren, Katie J. Wolfe
Protein conformational maladies such as Huntington Disease are characterized by accumulation of intracellular and extracellular protein inclusions containing amyloid-like proteins. There is an inverse correlation between proteotoxicity and aggregation, so facilitated protein aggregation appears cytoprotective. To define mechanisms for protective protein aggregation, …
Douglas Cyr, Hong Yu Ren, Katie J. Wolfe, Daniel W. Summers
Mechanisms for cooperation between the cytosolic Hsp70 system and the ubiquitin proteasome system during protein triage are not clear. Herein, we identify new mechanisms for selection of misfolded cytosolic proteins for degradation via defining functional interactions between specific cytosolic Hsp70/Hsp40 pairs and …
Martin Arthur Moseley, Dorothy A. Erie, George L. Sutphin, J. Will Thompson et autres
Transcription errors occur in all living cells; however, it is unknown how these errors affect cellular health. To answer this question, we monitored yeast cells that were genetically engineered to display error-prone transcription. We discovered that these cells suffer from a profound …
Philipp Trepte, Hong Yu Rena, Douglas Cyr, Katie J. Wolfe
Escape of aberrant proteins from protein quality control leads to accumulation of toxic protein species. Sti1 interacts with Hsp70 to mediate spatial PQC of amyloid-like proteins by regulating their distribution in different intracellular protein-handling depots. Sti1 suppresses proteotoxicity by targeting amyloid-like proteins …
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The accumulation of amyloid-like aggregates is a characteristic of protein conformational disorders such as Huntington Disease, but whether amyloid-like aggregation is causative or a cytoprotective mechanism remains unclear. Molecular chaperones act as the front line of defense against proteotoxicity, as they protect …
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Marc Vermulst, Ashley S. Denney, Michael J. Lang, Chao-Wei Hung et autres
Nature Communications 6, Article number: 8065 (2015); Published 25 August 2015; Updated 14 October 2015 The original version of this Article contained an error in the spelling of the authors J. Will Thompson and M. Arthur Moseley, which were incorrectly given as …
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Marc Vermulst, Ashley S. Denney, Michael J. Lang, Chao-Wei Hung et autres
Transcription errors occur in all living cells; however, it is unknown how these errors affect cellular health. To answer this question, we monitor yeast cells that are genetically engineered to display error-prone transcription. We discover that these cells suffer from a profound …
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Katie J. Wolfe, Hong Yu Ren, Philipp Trepte, Douglas Cyr
Protein conformational maladies such as Huntington Disease are characterized by accumulation of intracellular and extracellular protein inclusions containing amyloid-like proteins. There is an inverse correlation between proteotoxicity and aggregation, so facilitated protein aggregation appears cytoprotective. To define mechanisms for protective protein aggregation, …
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Katie J. Wolfe, Hong Yu Ren, Philipp Trepte, Douglas Cyr
Conformational diseases are associated with the conversion of normal proteins into aggregation-prone toxic conformers with structures similar to that of β-amyloid. Spatial distribution of amyloid-like proteins into intracellular quality control centers can be beneficial, but cellular mechanisms for protective aggregation remain unclear. …
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Daniel W. Summers, Katie J. Wolfe, Hong Yu Ren, Douglas Cyr
Mechanisms for cooperation between the cytosolic Hsp70 system and the ubiquitin proteasome system during protein triage are not clear. Herein, we identify new mechanisms for selection of misfolded cytosolic proteins for degradation via defining functional interactions between specific cytosolic Hsp70/Hsp40 pairs and …
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Daniel W. Summers, Katie J. Wolfe, Douglas Cyr
This chapter contains sections titled: Abbreviations Introduction Amyloid Formation in Disease Prion Propagation and Toxicity Functional Amyloid in Nature Conclusion and Future Directions Acknowledgment References
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