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HSP70-HSP90 chaperone networking in protein-misfolding disease
chapter
posted on 2023-06-10, 07:05 authored by Chrisostomos ProdromouChrisostomos Prodromou, Xavier Aran GuiuXavier Aran Guiu, Jasmeen OberoiJasmeen Oberoi, Laura Perna, J Paul Chapple, Jacqueline van der SpuyMolecular chaperones and their associated co-chaperones are essential in health and disease as they are key facilitators of protein-folding, quality control and function. In particular, the heat-shock protein (HSP) 70 and HSP90 molecular chaperone networks have been associated with neurodegenerative diseases caused by aberrant protein-folding. The pathogenesis of these disorders usually includes the formation of deposits of misfolded, aggregated protein. HSP70 and HSP90, plus their co-chaperones, have been recognised as potent modulators of misfolded protein toxicity, inclusion formation and cell survival in cellular and animal models of neurodegenerative disease. Moreover, these chaperone machines function not only in folding but also in proteasome-mediated degradation of neurodegenerative disease proteins. This chapter gives an overview of the HSP70 and HSP90 chaperones, and their respective regulatory co-chaperones, and explores how the HSP70 and HSP90 chaperone systems form a larger functional network and its relevance to counteracting neurodegenerative disease associated with misfolded proteins and disruption of proteostasis.
History
Publication status
- Published
Journal
Subcell BiochemISSN
0306-0225Publisher
Springer International PublishingExternal DOI
Volume
101Page range
389-425Event location
United StatesBook title
The Networking of Chaperones by Co-ChaperonesISBN
9783031147401Department affiliated with
- Biochemistry Publications
Full text available
- No
Peer reviewed?
- Yes
Editors
Gregory L Blatch, Adrienne L EdkinsLegacy Posted Date
2023-05-19Usage metrics
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