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Cdc37 as a Co-chaperone to Hsp90

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The Networking of Chaperones by Co-Chaperones

Part of the book series: Subcellular Biochemistry ((SCBI,volume 101))

Abstract

The co-chaperone p50/Cdc37 is an important partner for Hsp90, assisting in molecular chaperone activities, particularly with regard to the regulation of protein kinases. Analysis of the structure of Hsp90-Cdc37-kinase complexes demonstrates the way in which Cdc37 interacts with and controls the folding of a large proportion of intracellular protein kinases. This co-chaperone thus stands at the hub of a multitude of intracellular signaling networks. Indeed, the influence of Cdc37 reaches beyond the housekeeping pathways of protein folding into the regulation of a wide range of cellular processes. This co-chaperone has attracted attention as a potential intermediate in carcinogenesis. Cdc37 is an attractive potential target in cancer due to (1) high expression in a number of tumor types and (2) control of multiple signaling pathways. These properties indicate (3) a potential for selectivity due to its elevated expression in malignant cells and (4) robustness, as the co-chaperone may control multiple growth signaling pathways and thus be less prone to evolution of resistance than less versatile oncoproteins. Cdc37 may also be involved in other aspects of pathophysiology and has been shown to be secreted in exosomes. Protein aggregation disorders have been linked to age-related declines in molecular chaperones and co-chaperones. Cdc37 also appears to be a potential agent in longevity due to its links to protein folding and autophagy, and it will be informative to study the role of Cdc37 maintenance/decline in aging organisms.

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Acknowledgments

#This work was supported by NIH research grants RO-1CA047407, R01CA119045, and RO-1CA094397.

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Author notes

  1. Author Contributions: The review was conceived by Stuart K. Calderwood, and each author contributed equally to decision on content, writing, and figure creation.

Authors and Affiliations

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

    Thomas L. Prince, Benjamin J. Lang, Yuka Okusha & Stuart K. Calderwood

  2. Ranok Therapeutics, Waltham, MA, USA

    Thomas L. Prince

  3. Department of Dental Pharmacology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan

    Takanori Eguchi

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  1. Thomas L. Prince
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Correspondence to Stuart K. Calderwood .

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Editors and Affiliations

  1. Biomedical Biotechnology Research Unit, Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, South Africa

    Adrienne L. Edkins

  2. Faculty of Health Sciences, Higher Colleges of Technology, Sharjah, United Arab Emirates

    Gregory L. Blatch

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Prince, T.L., Lang, B.J., Okusha, Y., Eguchi, T., Calderwood, S.K. (2023). Cdc37 as a Co-chaperone to Hsp90. In: Edkins, A.L., Blatch, G.L. (eds) The Networking of Chaperones by Co-Chaperones. Subcellular Biochemistry, vol 101. Springer, Cham. https://doi.org/10.1007/978-3-031-14740-1_5

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