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首页> 外文期刊>Journal of cellular biochemistry. >Cholesterol inhibits the nuclear entry of estrogen receptor activation factor (E-RAF) and its dimerization with the nonactivated estrogen receptor (naER) in goat uterus.
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Cholesterol inhibits the nuclear entry of estrogen receptor activation factor (E-RAF) and its dimerization with the nonactivated estrogen receptor (naER) in goat uterus.

机译：胆固醇抑制山羊子宫中雌激素受体活化因子（E-RAF）的核进入及其与非活化雌激素受体（naER）的二聚作用。

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摘要

An alternative form of estrogen receptor isolated from goat uterus, the nonactivated estrogen receptor (naER), has no DNA-binding function, although it is closely similar to the classical estrogen receptor (ER) in its hormone binding affinity and specificity. The naER dimerizes with a DNA binding protein, estrogen receptor activation factor (E-RAF). The heterodimer binds to the DNA. Assays carried out during the purification of E-RAF showed that an endogenous inhibitor that is heat stable and dialyzable bound to the E-RAF and prevented the formation of the heterodimer. The inhibitor has been isolated and purified. GC-MS analysis identifies this molecule to be cholesterol. Circular dichroism measurement has shown that the high-affinity binding of cholesterol to E-RAF results in subtle changes in the secondary and the tertiary structure of the protein. The E-RAF with altered conformation fails to dimerize with the naER. Instead of facilitating E-RAF entry into the nucleus, dimerization with the naER prevents it. Similarly, cholesterol binding blocks the nuclear entry of the protein, showing that E-RAF with altered conformation is incapable of interaction with the nuclear pore complex/membrane proteins. The naER-E-RAF heterodimer remains at the nuclear periphery, incapable of further transport. These results indicate the possibility that the dimerization between naER and the E-RAF takes place only within the nuclear compartment. The observation that cholesterol binding prevents nuclear entry of the E-RAF reflects the similarity of E-RAF with the sterol regulatory element (SRE) binding protein that enters the nucleus and binds to SRE only when the intracellular level of cholesterol remains low. Copyright 2000 Wiley-Liss, Inc.
机译：从山羊子宫分离出的另一种形式的雌激素受体，即未激活的雌激素受体（naER），没有DNA结合功能，尽管在激素结合亲和力和特异性方面与经典雌激素受体（ER）非常相似。 naER通过DNA结合蛋白雌激素受体激活因子（E-RAF）来二聚。异二聚体与DNA结合。在纯化E-RAF的过程中进行的分析表明，热稳定且可透析的内源性抑制剂与E-RAF结合并阻止了异二聚体的形成。该抑制剂已被分离和纯化。 GC-MS分析确定该分子为胆固醇。圆二色性测量表明，胆固醇与E-RAF的高亲和力结合会导致蛋白质的二级和三级结构发生细微变化。构象改变的E-RAF不能与naER二聚。而不是促进E-RAF进入细胞核，用naER进行二聚化阻止了它的发生。同样，胆固醇结合会阻止蛋白质的核进入，这表明具有改变构象的E-RAF无法与核孔复合物/膜蛋白相互作用。 naER-E-RAF异二聚体保留在核外围，无法进一步运输。这些结果表明，naER和E-RAF之间仅在核室内发生二聚化的可能性。胆固醇结合阻止E-RAF核进入的观察反映了E-RAF与进入细胞核并仅在细胞内胆固醇水平保持低水平时与SRE结合的固醇调节元件（SRE）结合蛋白的相似性。版权所有2000 Wiley-Liss，Inc.

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