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Chaperone Regulation of the Heat Shock Protein Response

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Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 594))

Abstract

The heat shock protein response appears to be triggered primarily by nonnative proteins accumulating in a stressed cell and results in increased expression of heat shock proteins (HSPs). Many heat shock proteins prevent protein aggregation and participate in refolding or elimination of misfolded proteins in their capacity as chaperones. Even though several mechanisms exist to regulate the abundance of cytosolic and nuclear chaperones, activation of heat shock transcription factor 1 (HSF1) is an essential aspect of the heat shock protein response. HSPs and co-chaperones that are assembled into multichaperone complexes regulate HSF1 activity at different levels. HSP90-containing multichaperone complexes appear to be the most relevant repressors of HSF1 activity. Because HSP90-containing multichaperone complexes interact not only specifically with client proteins including HSF1 but also generically with nonnative proteins, the concentration of nonnative proteins influences assembly on HSF1 of HSP90-containing complexes that repress activation, and may play a role in inactivation, of the transcription factor. Proteins that are unable to achieve stable tertiary structures and remain chaperone substrates are targeted for proteasomal degradation through polyubiquitination by co-chaperone CHIP. CHIP can activate HSF1 to regulate the protein quality control system that balances protection and degradation of chaperone substrates.

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Authors and Affiliations

  1. HSF Pharmaceuticals SA, Avenue des Cerisiers 39B, 1009, Pully, Switzerland

    Richard Voellmy

  2. Carolina Cardiovascular Biology Center School of Medicine, University of North Carolina, Chapel Hill, North Carolina, USA

    Frank Boellmann

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  1. Department of Medical Chemistry, Semmelweis University, Budapest, Hungary

    Peter Csermely

  2. Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, Szeged, Hungary

    László Vígh

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Voellmy, R., Boellmann, F. (2007). Chaperone Regulation of the Heat Shock Protein Response. In: Csermely, P., Vígh, L. (eds) Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks. Advances in Experimental Medicine and Biology, vol 594. Springer, New York, NY. https://doi.org/10.1007/978-0-387-39975-1_9

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