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FEBS Lett. 2001 Apr 20;495(1-2):1-6.

Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases.

Author information

1
Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120, Halle/Saale, Germany. schiene@enzyme-halle.mpg.de

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.

PMID:
11322937
DOI:
10.1016/s0014-5793(01)02326-2
[Indexed for MEDLINE]
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