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The Role of p23, Hop, Immunophilins, and Other Co-chaperones in Regulating Hsp90 Function

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Molecular Chaperones

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

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 (1). 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

J.L.J. is funded by a grant from the National Science Foundation MCB-0744522. 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, El Paso, TX, USA

    Marc B. Cox

  2. Border Biomedical Research Center, El Paso, TX, USA

    Marc B. Cox

  3. Department of Microbiology, Molecular Biology, and Biochemistry, University of Idaho, Moscow, ID, 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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Editors and Affiliations

  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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Cox, M.B., Johnson, J.L. (2011). The Role of p23, Hop, Immunophilins, and Other Co-chaperones in Regulating Hsp90 Function. 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_4

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  • DOI: https://doi.org/10.1007/978-1-61779-295-3_4

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  • Print ISBN: 978-1-61779-294-6

  • Online ISBN: 978-1-61779-295-3

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