TY - JOUR
T1 - Association of the dioxin receptor with the Mr 90,000 heat shock protein
T2 - A structural kinship with the glucocorticoid receptor
AU - Denis, Marc
AU - Cuthill, Scott
AU - Wikström, Ann Charlotte
AU - Poellinger, Lorenz
AU - Gustafsson, Jan Åke
N1 - Funding Information:
This study was supported by grants from the Swedish Cancer Society and the National Institutes of Health (ESO 3954-01). SC is recipient of a training grant from the Swedish National Sciences Research Council. ACW and LP are recipients of research fellowships from the Swedish Medical Research Council.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1988/9/15
Y1 - 1988/9/15
N2 - The Mr ≈ 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.
AB - The Mr ≈ 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.
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U2 - 10.1016/S0006-291X(88)80566-7
DO - 10.1016/S0006-291X(88)80566-7
M3 - Article
C2 - 2844180
AN - SCOPUS:0023741595
SN - 0006-291X
VL - 155
SP - 801
EP - 807
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -