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

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Denis M,Cuthill S,Wikström AC,Poellinger L,Gustafsson JA

doi

10.1016/s0006-291x(88)80566-7

subject

Has Abstract

pub_date

1988-09-15 00:00:00

pages

801-7

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(88)80566-7

journal_volume

155

pub_type

杂志文章

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