J Proteins Counteract Amyloid Propagation and Toxicity in Yeast
The accumulation of misfolded proteins as amyloids is associated with pathology in dozens of debilitating human disorders, including diabetes, Alzheimer’s, Parkinson’s, and Huntington’s diseases. Expressing human amyloid-forming proteins in yeast is toxic, and yeast prions that propagate as infectio...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-08-01
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| Series: | Biology |
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| Online Access: | https://www.mdpi.com/2079-7737/11/9/1292 |
| _version_ | 1797490985400270848 |
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| author | Daniel C. Masison Michael Reidy Jyotsna Kumar |
| author_facet | Daniel C. Masison Michael Reidy Jyotsna Kumar |
| author_sort | Daniel C. Masison |
| collection | DOAJ |
| description | The accumulation of misfolded proteins as amyloids is associated with pathology in dozens of debilitating human disorders, including diabetes, Alzheimer’s, Parkinson’s, and Huntington’s diseases. Expressing human amyloid-forming proteins in yeast is toxic, and yeast prions that propagate as infectious amyloid forms of cellular proteins are also harmful. The yeast system, which has been useful for studying amyloids and their toxic effects, has provided much insight into how amyloids affect cells and how cells respond to them. Given that an amyloid is a protein folding problem, it is unsurprising that the factors found to counteract the propagation or toxicity of amyloids in yeast involve protein quality control. Here, we discuss such factors with an emphasis on J-domain proteins (JDPs), which are the most highly abundant and diverse regulators of Hsp70 chaperones. The anti-amyloid effects of JDPs can be direct or require interaction with Hsp70. |
| first_indexed | 2024-03-10T00:40:55Z |
| format | Article |
| id | doaj.art-1b2ad10dd67947b398f93156ebccfab0 |
| institution | Directory Open Access Journal |
| issn | 2079-7737 |
| language | English |
| last_indexed | 2024-03-10T00:40:55Z |
| publishDate | 2022-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biology |
| spelling | doaj.art-1b2ad10dd67947b398f93156ebccfab02023-11-23T15:07:05ZengMDPI AGBiology2079-77372022-08-01119129210.3390/biology11091292J Proteins Counteract Amyloid Propagation and Toxicity in YeastDaniel C. Masison0Michael Reidy1Jyotsna Kumar2Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USALaboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USADepartment of Chemistry, University of Connecticut, Storrs, CT 06269, USAThe accumulation of misfolded proteins as amyloids is associated with pathology in dozens of debilitating human disorders, including diabetes, Alzheimer’s, Parkinson’s, and Huntington’s diseases. Expressing human amyloid-forming proteins in yeast is toxic, and yeast prions that propagate as infectious amyloid forms of cellular proteins are also harmful. The yeast system, which has been useful for studying amyloids and their toxic effects, has provided much insight into how amyloids affect cells and how cells respond to them. Given that an amyloid is a protein folding problem, it is unsurprising that the factors found to counteract the propagation or toxicity of amyloids in yeast involve protein quality control. Here, we discuss such factors with an emphasis on J-domain proteins (JDPs), which are the most highly abundant and diverse regulators of Hsp70 chaperones. The anti-amyloid effects of JDPs can be direct or require interaction with Hsp70.https://www.mdpi.com/2079-7737/11/9/1292J proteinsamyloidpolyglutamineprions |
| spellingShingle | Daniel C. Masison Michael Reidy Jyotsna Kumar J Proteins Counteract Amyloid Propagation and Toxicity in Yeast Biology J proteins amyloid polyglutamine prions |
| title | J Proteins Counteract Amyloid Propagation and Toxicity in Yeast |
| title_full | J Proteins Counteract Amyloid Propagation and Toxicity in Yeast |
| title_fullStr | J Proteins Counteract Amyloid Propagation and Toxicity in Yeast |
| title_full_unstemmed | J Proteins Counteract Amyloid Propagation and Toxicity in Yeast |
| title_short | J Proteins Counteract Amyloid Propagation and Toxicity in Yeast |
| title_sort | j proteins counteract amyloid propagation and toxicity in yeast |
| topic | J proteins amyloid polyglutamine prions |
| url | https://www.mdpi.com/2079-7737/11/9/1292 |
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