The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo

Daniel L. Riggs, Patricia J. Roberts, Samantha C. Chirillo, Joyce Cheung-Flynn, Viravan Prapapanich, Thomas Ratajczak, Richard Gaber, Didier Picard, David F. Smith*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

273 Scopus citations


Hsp90 is required for the normal activity of steroid receptors, and in steroid receptor complexes it is typically bound to one of the immunophilin-related cochaperones: the peptidylprolyl isomerases FKBP51, FKBP52 or CyP40, or the protein phosphatase PP5. The physiological roles of the immunophilins in regulating steroid receptor function have not been well defined, and so we examined in vivo the influences of immunophilins on hormone-dependent gene activation in the Saccharomyces cerevisiae model for glucocorticoid receptor (GR) function. FKBP52 selectively potentiates hormone-dependent reporter gene activation by as much as 20-fold at limiting hormone concentrations, and this potentiation is readily blocked by co-expression of the closely related FKBP51. The mechanism for potentiation is an incgease in GR hormone-binding affinity that requires both the Hsp90-binding ability and the prolyl isomerase activity of FKBP52.

Original languageEnglish (US)
Pages (from-to)1158-1167
Number of pages10
JournalEMBO Journal
Issue number5
StatePublished - Mar 3 2003


  • FKBP52
  • Glucocorticoid receptor
  • Hsp90
  • Immunophilin
  • Peptidylprolyl isomerase

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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