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FKBP52.

Todd H Davies1, Edwin R Sánchez

  • 1Department of Pharmacology, Medical College of Ohio, 3035 Arlington Avenue, Toledo, OH 43614-5804, USA.

The International Journal of Biochemistry & Cell Biology
|September 24, 2004
PubMed
Summary

FKBP52, an immunophilin, has peptidyl-prolyl cis-trans isomerase (PPIase) activity. Its tetratricopeptide repeat (TPR) domains bind Hsp90, influencing steroid receptor signaling and other cellular roles.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • FKBP52 is a large molecular-weight immunophilin targeted by FK506.
  • It shares peptidyl-prolyl cis-trans isomerase (PPIase) activity with FKBP12, inhibited by FK506.
  • Unlike FKBP12, FKBP52 does not mediate FK506's immunosuppressive effects.

Purpose of the Study:

  • To review the structural features of FKBP52.
  • To relate these structures to the protein's diverse and evolving functions.
  • To discuss both recognized and less-known roles of FKBP52.

Main Methods:

  • Literature review of structural and functional studies on FKBP52.
  • Analysis of FKBP52's molecular weight and domain composition.
  • Comparison of FKBP52 with FKBP12.

Main Results:

  • FKBP52 possesses multiple functional domains beyond PPIase activity.
  • Tetratricopeptide repeat (TPR) domains are key structural features.
  • These TPR domains act as binding sites for the molecular chaperone Hsp90.

Conclusions:

  • FKBP52's TPR domains and Hsp90 binding are central to its cellular functions.
  • The primary recognized role of FKBP52 is in regulating steroid receptor signaling.
  • FKBP52 exhibits diverse functions beyond its interaction with FK506 and steroid receptors.

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