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首页> 外文期刊>Molecular and Cellular Endocrinology >Membrane estrogen receptors: genomic actions and post transcriptional regulation.
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Membrane estrogen receptors: genomic actions and post transcriptional regulation.

机译:膜雌激素受体:基因组作用和转录后调控。

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The primary cellular location of the nuclear estrogen receptor II (nER II) is the plasma membrane. A number of reports that have appeared in the recent past indicate that plasma membrane localized estrogen receptor alpha (ERalpha) also exists. Whether the membrane localized ERalpha represents the receptor that binds to the estrogen responsive element (ERE) remains to be known. The mechanisms that underlie the internalization of nER II (non-activated estrogen receptor, deglycosylated) have been identified to a certain extent. The question remains: is the primary location of the ERalpha also the plasma membrane? If that is the case, it will be a challenging task to identify the molecular events that underlie the plasma membrane-to-nucleus movement of ERalpha. The internalization mechanisms for the two 66kDa plasma membrane ERs, following hormone binding, appear to be distinct and without any overlaps. Interestingly, while the major gene regulatory role for ERalpha appears to be at the level of transcription, the nER II has its major functional role in post transcriptional mechanisms. The endoplasmic reticulum associated anchor protein-55 (ap55) that was recently reported from the author's laboratory needs a closer look. It is a high affinity estrogen binding protein that anchors the estrogen receptor activation factor (E-RAF) in an estrogen-mediated event. It will be interesting to examine whether ap55 bears any structural similarity with either ERalpha or ERbeta.
机译:核雌激素受体II(nER II)的主要细胞位置是质膜。最近出现的许多报告表明,也存在质膜定位的雌激素受体α(ERalpha)。膜定位的ERα是否代表与雌激素反应性元件(ERE)结合的受体尚不清楚。 nER II(非活化的雌激素受体,去糖基化)内在化的机制已得到一定程度的确认。问题仍然存在:ERalpha的主要位置还是质膜吗?如果真是这样,要确定构成ERalpha质膜-核运动基础的分子事件,将是一项艰巨的任务。在激素结合后,两个66kDa质膜内质网的内在化机制似乎是不同的,没有任何重叠。有趣的是,虽然ERalpha的主要基因调控作用似乎在转录水平,但nER II在转录后机制中具有其主要功能。作者实验室最近报道的内质网相关锚蛋白55(ap55)需要仔细观察。它是一种高亲和力的雌激素结合蛋白,可在雌激素介导的事件中锚定雌激素受体激活因子(E-RAF)。检查ap55是否与ERalpha或ERbeta具有任何结构相似性将是很有趣的。

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