Abstract
Hsp70 and Hsp90 are molecular chaperones (heat shock proteins) that facilitate client protein maturation, stabilization of aggregation-prone proteins, quality control of misfolded proteins and maintenance of proteins in an activation-competent conformation. In general, these Hsps are part of the cellular proteostasis network that functions in normal and disease states to maintain protein homeostasis. Recent data suggest a role for certain components of the proteostasis network (e.g., the proteasome) in various aspects of immune responses, and lately molecular chaperones have also been suggested to play a role in immunity, although the exact nature of their function remains somewhat controversial. Given the growing importance of Hsp90 and Hsp70 in a number of different diseases, including cancer and neurodegenerative maladies, as well as their role in contributing to protein homeostasis in health and disease, pharmacologic targetingĀ of Hsp70, Hsp90 and their respective co-chaperones remains an area of intense investigation, although the impact of Hsp inhibition on immune cells and systems remains poorly understood.
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Moses, M.A., Zuehlke, A.D., Neckers, L. (2018). Molecular Chaperone Inhibitors. In: Binder, R., Srivastava, P. (eds) Heat Shock Proteins in the Immune System. Springer, Cham. https://doi.org/10.1007/978-3-319-69042-1_2
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