Work

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

Year: 2001

Type: review

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.

Source: FEBS Letters

DOI: 10.1016/s0014-5793(01)02326-2

Authors: Cordelia Schiene-Fischer, Chao Yu

Institution: Max Planck Research Unit for Enzymology of Protein Folding

Language: English

Topic: Signaling Pathways in Disease

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

OpenAlex ID: W2093693347

FWCI: 1.025

Cites: 65

Cited by: 184

Related to: 10