Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases
- 19 April 2001
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 495 (1-2) , 1-6
- https://doi.org/10.1016/s0014-5793(01)02326-2
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.Keywords
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