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

被引:156
作者
Schiene-Fischer, C [1 ]
Yu, C [1 ]
机构
[1] Max Planck Res Unit Enzymol Prot Folding, D-06120 Halle, Germany
关键词
peptidyl prolyl cis/trans isomerase; steroid receptor; calcium channel; receptor protein kinase;
D O I
10.1016/S0014-5793(01)02326-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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, (C) 2001 Federation of European Biochemical Societies, Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:1 / 6
页数:6
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