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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade
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Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade

机译：与Src / Erk磷酸化级联反应调节其非基因组活性串扰的雌激素受体相互作用蛋白

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Numerous studies have demonstrated that estrogens induce rapid and transient activation of the Src/Erk phosphorylation cascade. Activation of this cascade triggers vital cellular functions including cell proliferation and differentiation. However, the details of the molecular mechanism of this process remain to be elucidated. We have identified a previously uncharacterized nuclear receptor-interacting protein designated as modulator of nongenomic activity of estrogen receptor (MNAR). Here we show that MNAR modulates estrogen-receptor (ER) interaction with members of the Src family of tyrosine kinases, which leads to a stimulation of Src enzymatic activity and activation of Erk1 and Erk2 kinases. We also show that MNAR, through activation of the Src/Erk phosphorylation cascade, affects ER transcriptional activity and ultimately ER-mediated gene expression. These data reveal that MNAR mediates the crosstalk between two important classes of signal transducing molecules and suggest that ER "genomic" and "nongenomic" activities are interrelated.
机译：大量研究表明，雌激素可诱导Src / Erk磷酸化级联反应的快速和短暂激活。该级联反应的激活触发重要的细胞功能，包括细胞增殖和分化。但是，该过程的分子机理的细节仍有待阐明。我们已经确定了以前未被表征的核受体相互作用蛋白，被指定为雌激素受体（MNAR）非基因组活性的调节剂。在这里，我们显示MNAR调节与雌激素受体酪氨酸激酶Src家族成员的雌激素受体（ER）相互作用，从而刺激Src酶活性并激活Erk1和Erk2激酶。我们还显示，通过激活Src / Erk磷酸化级联，MNAR影响ER转录活性，并最终影响ER介导的基因表达。这些数据表明，MNAR介导了两类重要的信号转导分子之间的串扰，并表明ER的“基因组”和“非基因组”活动是相互关联的。

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