Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases.
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.
Schiene-Fischer
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Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120, Halle/Saale, Germany. schiene@enzyme-halle.mpg.de
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D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D000081406:Peptidyl-Prolyl Isomerase F; D021983:Cyclophilins; D018841:HSP90 Heat-Shock Proteins; D006801:Humans; D046911:Macromolecular Substances; D051379:Mice; D019696:Peptidylprolyl Isomerase / Q000378:metabolism*; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000502:physiology; D011956:Receptors, Cell Surface / Q000378:metabolism*; D018160:Receptors, Cytoplasmic and Nuclear / Q000378:metabolism*; D022021:Tacrolimus Binding Proteins / Q000378:metabolism
D002352:Carrier Proteins; D000081406:Peptidyl-Prolyl Isomerase F; D018841:HSP90 Heat-Shock Proteins; D046911:Macromolecular Substances; C000631446:PPIF protein, mouse; D011956:Receptors, Cell Surface; D018160:Receptors, Cytoplasmic and Nuclear; D021983:Cyclophilins; D022021:Tacrolimus Binding Proteins; D019696:Peptidylprolyl Isomerase