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Receptor accessory folding helper enzymes: the functional role of peptidyl prolylcis/transisomerases

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
495
Identifiers
DOI: 10.1016/s0014-5793(01)02326-2
Keywords
  • Peptidyl Prolylcis/Transisomerase
  • Steroid Receptor
  • Calcium Channel
  • Receptor Protein Kinase
Disciplines
  • Biology

Abstract

Abstract Receptor accessory peptidyl prolyl cis/ trans isomerases (PPIases) of the FKBP and cyclophilin types form receptor heterocomplexes with different stabilities. PPIases have been found to associate with other receptor heterocomplex constituents via either proline-directed active sites or additional domains of the enzymes. The single-domain PPIases FKBP12 and FKBP12.6 are shown to interact with receptor protein kinases and calcium channels at their active sites. In contrast, heterooligomeric nuclear receptors contain multi-domain PPIases like FKBP51, FKBP52 or cyclophilin 40 that directly interact with the chaperone hsp90 via the tetratricopeptide repeat modules of the folding helper enzymes. PPIases play a critical role in the functional arrangement of components within receptor heterocomplexes.

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