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The Role of HSP70 and Its Co-chaperones in Protein Misfolding, Aggregation and Disease

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The Networking of Chaperones by Co-chaperones

Part of the book series: Subcellular Biochemistry ((SCBI,volume 78))

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 HSP70 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 its co-chaperones have been recognised as potent modulators of inclusion formation and cell survival in cellular and animal models of neurodegenerative disease. In has become evident that the HSP70 chaperone machine functions not only in folding, but also in proteasome mediated degradation of neurodegenerative disease proteins. Thus, there has been a great deal of interest in the potential manipulation of molecular chaperones as a therapeutic approach for many neurodegenerations. Furthermore, mutations in several HSP70 co-chaperones and putative co-chaperones have been identified as causing inherited neurodegenerative and cardiac disorders, directly linking the HSP70 chaperone system to human disease.

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Acknowledgements

The text in this chapter contains sections reproduced with kind permission from Springer Science + Business Media: Networking of Chaperones by Co-chaperones; Chap. 11: The role of Hsp70 and its co-chaperones in protein misfolding, aggregation and disease; 2007; page 122–127; Jacqueline van der Spuy, Michael E, Cheetham and J. Paul Chapple.

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Authors and Affiliations

  1. Molecular Endocrinology Centre, William Harvey Research Institute, Barts and the London School of Medicine and Dentistry, Queen Mary University of London, Charter House Square, EC1M 6BQ, London, UK

    Emma J. Duncan & J. Paul Chapple

  2. Department of Ocular Biology and Therapeutics, UCL Institute of Ophthalmology, 11–43 Bath Street, EC1V 9EL, London, UK

    Michael E. Cheetham & Jacqueline van der Spuy

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  1. Emma J. Duncan
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  2. Michael E. Cheetham
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  3. J. Paul Chapple
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  4. Jacqueline van der Spuy
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Correspondence to J. Paul Chapple or Jacqueline van der Spuy .

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  1. Victoria University, College of Health and Biomedicine, Melbourne, Victoria, Australia

    Gregory Lloyd Blatch

  2. Department of Biochemistry and Microbiology, Rhodes University, Biomedical Biotechnology Research Unit, Grahamstown, South Africa

    Adrienne Lesley Edkins

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Duncan, E., Cheetham, M., Chapple, J., van der Spuy, J. (2015). The Role of HSP70 and Its Co-chaperones in Protein Misfolding, Aggregation and Disease. In: Blatch, G., Edkins, A. (eds) The Networking of Chaperones by Co-chaperones. Subcellular Biochemistry, vol 78. Springer, Cham. https://doi.org/10.1007/978-3-319-11731-7_12

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