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

FEBS Letters

Schiene-Fischer, Cordelia¹  Yu, Chao¹ 

[1] Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale, Germany

关键词: Peptidyl prolyl cis/trans isomerase;    Steroid receptor;    Calcium channel;    Receptor protein kinase;    AhR;    arylhydrocarbon receptor;    CsA;    cyclosporin A;    Cyp;    cyclophilin;    EGF;    epidermal growth factor;    FKBP;    FK506 binding protein;    GR;    glucocorticoid receptor;    PPIase;    peptidyl prolyl cis/trans isomerase;    PR;    progesterone receptor;    RyR;    ryanodine receptor;    TC;    terminal cisternae;    TβR;    TGF-β receptor;    TGF-β;    transforming growth factor-β;    TPR;    tetratricopeptide repeat;   

DOI  :  10.1016/S0014-5793(01)02326-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown