ASSOCIATION OF THE DIOXIN RECEPTOR WITH THE MR 90,000 HEAT-SHOCK PROTEIN - A STRUCTURAL KINSHIP WITH THE GLUCOCORTICOID RECEPTOR
ASSOCIATION OF THE DIOXIN RECEPTOR WITH THE MR 90,000 HEAT-SHOCK PROTEIN - A STRUCTURAL KINSHIP WITH THE GLUCOCORTICOID RECEPTOR
复制标题
DOI：
10.1016/s0006-291x(88)80566-7
复制
发表时间：
1988-09-15
影响因子：
3.1
通讯作者：
GUSTAFSSON, JA
中科院分区：
文献类型：
--
作者：
DENIS, M;CUTHILL, S;GUSTAFSSON, JA
西蒙先生。90，000热休克蛋白，hsp 890，容易与糖皮质激素受体相互作用，形成9 S，非DNA结合受体复合物。这种受体在胞质制剂中被β-氨基丁酸钠稳定。类似地，氰化钠可以稳定二恶英受体的9 S形式.多克隆抗体对纯化的糖皮质激素受体assocaited热休克蛋白90相互作用的稳定的9 S二恶英受体复合物，但不与4 S二恶英受体单体，作为评估的沉降位移分析蔗糖梯度。因此，我们得出结论，二恶英和糖皮质激素受体可以形成异聚复合物，其中共享一个共同的非配体结合组件。这些结果首次证明了二恶英和糖皮质激素受体之间的结构关系。
The Mr .simeq. 90,000 heat shock protein, hsp890, 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-assocaited 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.