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1. Introduction
2. Outcomes of misfolded protein aggregation
3. The study of neurodegenerative diseases
4. Regulation of Hsp70 function by Hsp40
5. Domain structure of Hsp40 family members
6. Functional specificity of Type I and Type II HSP40
7. Hsp70 and Hsp40s act via opposing mechanisms
8. Hsp40s differentially modulate fibril formation
9. RNQ+ as a model system for amyloid assembly
10. Rnq1 forms self-perpetuating aggregates
11. Hsp40 types - opposing roles on RNQ+ assembly
12. Sis1 and Ydj1 recognize different regions of Rnq1
13. Hsp40 types bind different regions of Rnq1 prions
14. Rnq1 elevation kills yeast containing RNQ+ prions
15. Overexpression of Sis1 suppresses Rnq1 toxicity
16. A possible mechanism for Rnq1 toxicity?
17. Sis1 decreases unassembled Rnq1 pool
18. Sis1 promotes RNQ prion accumulation
19. RNQ prion accumulation may help reduce toxicity
20. How type I Hsp40s suppress amyloid formation
21. Rnq1 prion domain overexpression in yeast
22. Ydj1 required for tolerance of PrD overexpression
23. Ydj1 overexpression inhibits PrD aggregation
24. PrD accumulation in the absence of Ydj1
25. A model for PRD prion formation
26. Hsp40s suppress proteotoxicity in different ways
27. Acknowledgements

Topics Covered

• Protein aggregation in conformational disease
• The Hsp40 system
• The Hsp70 system
• Small oligomers, prion, yeast, Huntington's disease and protein triage
• Mechanisms for proteotoxicity
• Mechanisms for amyloid disease

Links

Series:

• Protein Homeostasis

Categories:

• Biochemistry
• Cell Biology

Therapeutic Areas:

• Neurology

Talk Citation

Cyr, D.M. (2012, February 20). Roles for Hsp40 molecular chaperones in protein misfolding disease [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved November 23, 2024, from https://doi.org/10.69645/GMGJ2525.
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Publication History

• Published on February 20, 2012

Financial Disclosures

• Prof. Douglas M. Cyr has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.