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Chaperones pp 397–422Cite as

Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 1709))

Abstract

Molecular chaperones are a diverse group of highly conserved proteins that transiently interact with partially folded polypeptide chains during normal cellular processes such as protein translation, translocation, and disassembly of protein complexes. Prior to folding or after denaturation, hydrophobic residues that are normally sequestered within a folded protein are exposed to the aqueous environment and are prone to aggregation or misfolding. Multiple classes of molecular chaperones, such as Hsp70s and Hsp40s, recognize and transiently bind polypeptides with exposed hydrophobic stretches in order to prevent misfolding. Other types of chaperones, such as Hsp90, have more specialized functions in that they appear to interact with only a subset of cellular proteins. This chapter focuses on the role of Hsp90 and partner co-chaperones in promoting the folding and activation of a diverse group of proteins with critical roles in cellular signaling and function.

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Acknowledgments

M.B.C. is supported in part by NIH/NIGMS grant No. 1SC1GM084863 and Grant Number 5G12RR008124 (to the Border Biomedical Research Center/University of Texas at El Paso) from the National Center for Research Resources (NCRR/NIH). The contents of this publication are solely the responsibility of the authors and do not necessarily represent the official views of NCRR or NIH.

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Authors and Affiliations

  1. Department of Biological Sciences, University of Texas at El Paso and the Border Biomedical Research Center, El Paso, TX, 79968, USA

    Marc B. Cox

  2. Department of Biological Sciences and the Center for Reproductive Biology, University of Idaho, Moscow, ID, 83844-3051, USA

    Jill L. Johnson

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  1. Marc B. Cox
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  2. Jill L. Johnson
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Correspondence to Jill L. Johnson .

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

    Stuart K. Calderwood

  2. Department of Urology, Weis Center for Research, Geisinger Clinic, Danville, Pennsylvania, USA

    Thomas L. Prince

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Cox, M.B., Johnson, J.L. (2018). Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding. In: Calderwood, S., Prince, T. (eds) Chaperones. Methods in Molecular Biology, vol 1709. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7477-1_28

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