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HSP70-HSP90 Chaperone Networking in Protein-Misfolding Disease

Prodromou, C; Aran-Guiu, X; Oberoi, J; Perna, L; Chapple, JP; van der Spuy, J; (2023) HSP70-HSP90 Chaperone Networking in Protein-Misfolding Disease. The Networking of Chaperones by Co-Chaperones: Subcellular Biochemistry , 101 pp. 389-425. 10.1007/978-3-031-14740-1_13. Green open access

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Abstract

Molecular 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.

Type: Article
Title: HSP70-HSP90 Chaperone Networking in Protein-Misfolding Disease
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1007/978-3-031-14740-1_13
Publisher version: https://doi.org/10.1007/978-3-031-14740-1_13
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
Keywords: Chaperone, Co-chaperones, HSP70, HSP90, Neurodegeneration, Protein degradation, Protein quality control, Animals, HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Molecular Chaperones, Neurodegenerative Diseases, Protein Folding
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > Institute of Ophthalmology
URI: https://discovery.ucl.ac.uk/id/eprint/10164275
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