Abstract
Hsp90 functionally interacts with a broad array of client proteins, but in every case examined Hsp90 is accompanied by one or more co-chaperones. One class of co-chaperone contains a tetratricopeptide repeat domain that targets the co-chaperone to the C-terminal region of Hsp90. Within this class are Hsp90-binding peptidylprolyl isomerases, most of which belong to the FK506-binding protein (FKBP) family. Despite the common association of FKBP co-chaperones with Hsp90, it is now clear that the client protein influences, and is influenced by, the particular FKBP bound to Hsp90. Examples include Xap2 in aryl hydrocarbon receptor complexes and FKBP52 in steroid receptor complexes. In this chapter, we discuss the known functional roles played by FKBP co-chaperones and, where possible, relate distinctive functions to structural differences between FKBP members.
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Acknowledgements
Studies in the authors’ laboratory were supported by grants to the Border Biomedical Research Center from the National Center for Research Resources (5 G12 RR008124) and from the National Institute on Minority Health and Health Disparities (8 G12 MD007592) from the National Institutes of Health. The authors were also supported in part by the Cancer Prevention and Research Institute of Texas by grant number RP110444-P2 (M.B.C). M.D.G. was supported by grants PICT 2011-1715, UBACYT 2011-14-GC, and the Fundación Roemmers. The text in this chapter contains sections reproduced with kind permission from Springer Science + Business Media: Networking of Chaperones by Co-chaperones; Chapter 2: Functions of the Hsp90-Binding FKBP Immunophilins; 2006; page 13–21; Marc B. Cox and David F. Smith
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Guy, N., Garcia, Y., Sivils, J., Galigniana, M., Cox, M. (2015). Functions of the Hsp90-Binding FKBP Immunophilins. In: Blatch, G., Edkins, A. (eds) The Networking of Chaperones by Co-chaperones. Subcellular Biochemistry, vol 78. Springer, Cham. https://doi.org/10.1007/978-3-319-11731-7_2
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