Duncan, EJ; Cheetham, ME; Chapple, JP; van der Spuy, J; (2015) The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease. Subcellular Biochemistry , 78 pp. 243-273. 10.1007/978-3-319-11731-7_12.

Text Cheetham_van der Spuy et al Text draft 2.pdf - Accepted Version Access restricted to UCL open access staff Available under License : See the attached licence file. Download (411kB)

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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