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Cellular Trafficking of Cell Stress Proteins in Health and Disease pp 167–183Cite as

Chaperonin 60: An Unexpected Cell Surface Receptor in Prokaryotes and Eukaryotes

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Part of the book series: Heat Shock Proteins ((HESP,volume 6))

Abstract

The chaperonin (Cpn)60 protein is a fascinating molecule which, under different circumstances, exists on the cell surface or is secreted from the cell. In all the various compartments in which the Cpn60 protein is found in organisms ranging from bacteria, to invertebrates to vertebrates it has evolved a wide range of additional, moonlighting, functions. Among the most unusual of these functions is the ability of this protein to exist on cell surfaces and act like a conventional agonist receptor. This chapter reviews the unexpected receptor and adhesive functions of the Cpn60 pantheon.

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  1. Department of Microbial Diseases, UCL-Eastman Dental Institute, University College London, 256 Gray’s Inn Road, WC1X 8LD, London, UK

    Prof. Brian Henderson

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  1. Eastman Dental Institute, Div. Microbial Diseases, University College, London, Gray's Inn Road 256, London, WC1X 8LD, United Kingdom

    Brian Henderson

  2. School of Medicine & Biomedical Science, University of Sheffield, Beech Hill Road, Sheffield, S10 2RX, United Kingdom

    A. Graham Pockley

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Henderson, B. (2012). Chaperonin 60: An Unexpected Cell Surface Receptor in Prokaryotes and Eukaryotes. In: Henderson, B., Pockley, A. (eds) Cellular Trafficking of Cell Stress Proteins in Health and Disease. Heat Shock Proteins, vol 6. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-4740-1_11

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