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Hsp90 and Client Protein Maturation

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Molecular Chaperones

Part of the book series: Methods in Molecular Biology ((MIMB,volume 787))

Abstract

Heat-shock protein 90 (Hsp90) is a molecular chaperone that assists in the maturation of a limited set of substrate proteins that are collectively referred to as clients. The majority of identified Hsp90 clients are involved in signal transduction, including many steroid hormone receptors and kinases. A handful of Hsp90 clients can be classified as nonsignal transduction proteins, including telomerase, cystic fibrosis transmembrane conductance regulator, and antigenic peptides destined for major histocompatibility complex. Because Hsp90 clients are causative agents in cancer and cystic fibrosis, research on Hsp90 has intensified in recent years. We review the historical path of Hsp90 research within each class of client (kinase, hormone receptor, and nonsignal transduction clients) and highlight current areas of active investigation.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA, USA

    Natalie Wayne, Parul Mishra & Daniel N. Bolon

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  1. Natalie Wayne
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  2. Parul Mishra
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  3. Daniel N. Bolon
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Correspondence to Daniel N. Bolon .

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  1. Beth Israel Deaconess Medical Center, Department of Radiation Oncology, Harvard Medical School, Brookline Ave 330, Boston, 02215, Massachusetts, USA

    Stuart K. Calderwood

  2. National Cancer Institute, Urologic Oncology Branch, National Institutes of Health, Rockville Pike 9000, Bethesda, 20814, Maryland, USA

    Thomas L. Prince

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Wayne, N., Mishra, P., Bolon, D.N. (2011). Hsp90 and Client Protein Maturation. In: Calderwood, S., Prince, T. (eds) Molecular Chaperones. Methods in Molecular Biology, vol 787. Humana Press. https://doi.org/10.1007/978-1-61779-295-3_3

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  • DOI: https://doi.org/10.1007/978-1-61779-295-3_3

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