Functions of the Hsp90-binding FKBP Immunophilins.

Publication Date


Document Type

Book Chapter


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


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.