Association of the dioxin receptor with the Mr 90,000 heat shock protein: a structural kinship with the glucocorticoid receptor

Biochem Biophys Res Commun. 1988 Sep 15;155(2):801-7. doi: 10.1016/s0006-291x(88)80566-7.


The Mr approximately equal to 90,000 heat shock protein, hsp90, readily interacts with the glucocorticoid receptor to form the 9 S, non-DNA-binding receptor complex. This receptor is stabilized in cytosolic preparations by sodium molybdate. In analogy, sodium molybdate stabilizes a 9 S form of the dioxin receptor. Polyclonal antibodies raised against the purified glucocorticoid receptor-associated hsp90 interact with the molybdate-stabilized 9 S dioxin-receptor complex but not with the 4 S dioxin receptor monomer, as assessed by sedimentation shift analysis on sucrose gradients. Thus we conclude that both the dioxin and glucocorticoid receptor can form heteromeric complexes which share a common non-ligand-binding component. These results represent the first demonstration of a structural relationship between the dioxin and glucocorticoid receptors.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Centrifugation, Density Gradient
  • Heat-Shock Proteins / analysis*
  • Humans
  • Liver / analysis
  • Molecular Weight
  • Placenta / analysis
  • Rats
  • Receptors, Aryl Hydrocarbon
  • Receptors, Drug / analysis*
  • Receptors, Glucocorticoid / analysis*


  • Heat-Shock Proteins
  • Receptors, Aryl Hydrocarbon
  • Receptors, Drug
  • Receptors, Glucocorticoid