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. 2023:101:41-80.
doi: 10.1007/978-3-031-14740-1_2.

Functions of the Hsp90-Binding FKBP Immunophilins

Nina R Ortiz  1 , Naihsuan Guy  1 , Yenni A Garcia  1 , Jeffrey C Sivils  1 , Mario D Galigniana  2   3 , Marc B Cox  4   5
Affiliations

Functions of the Hsp90-Binding FKBP Immunophilins

Nina R Ortiz et al. Subcell Biochem. 2023.

Abstract

The Hsp90 chaperone is known to interact with a diverse array of client proteins. However, in every case examined, Hsp90 is also accompanied by a single or several co-chaperone proteins. One class of co-chaperone contains a tetratricopeptide repeat (TPR) 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 abundantly clear that the client protein influences, and is often 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.

Keywords: Co-chaperone; FKBP; Hsp90; Immunophilin; Steroid hormone receptor; TPR domain.

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