Association of the dioxin receptor with the Mr 90,000 heat shock protein: a structural kinship with the glucocorticoid receptor.
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.
Denis
M
M
Department of Medical Nutrition, Karolinska Institute, Huddinge University Hospital, Sweden.
Cuthill
S
S
Wikström
A C
AC
Poellinger
L
L
Gustafsson
J A
JA
D000818:Animals; D002499:Centrifugation, Density Gradient; D006360:Heat-Shock Proteins / Q000032:analysis*; D006801:Humans; D008099:Liver / Q000032:analysis; D008970:Molecular Weight; D010920:Placenta / Q000032:analysis; D051381:Rats; D018336:Receptors, Aryl Hydrocarbon; D011955:Receptors, Drug / Q000032:analysis*; D011965:Receptors, Glucocorticoid / Q000032:analysis*
D006360:Heat-Shock Proteins; D018336:Receptors, Aryl Hydrocarbon; D011955:Receptors, Drug; D011965:Receptors, Glucocorticoid