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Science 29 May 1992:
Vol. 256. no. 5061, pp. 1315 - 1318
DOI: 10.1126/science.1376003
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Articles

Science, Vol 256, Issue 5061, 1315-1318
Copyright © 1992 by American Association for the Advancement of Science

articles

Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex

PK Tai, MW Albers, H Chang, LE Faber, and SL Schreiber

Department of Obstetrics and Gynecology, Medical College of Ohio, Toledo 43699.

Immunophilins, a family of proteins that exhibit rotamase (peptidyl-prolyl cis-trans isomerase) activity in vitro, are expressed in many organisms and most tissues. Although some immunophilins can mediate the immunosuppressive actions of FK506, rapamycin, and cyclosporin A, the physiological role of the unligated proteins is not known. A 59-kilodalton member of the FK506- and rapamycin-binding class was found to associate in the absence of these drugs with two heat shock proteins (hsp90 and hsp70) and the glucocorticoid receptor (GR). Together, these proteins make up the inactive GR, thus biochemically linking two families of proteins proposed to be involved in protein folding and assembly as well as two potent immunosuppressive modalities.


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