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首页> 外文期刊>Molecular and Cellular Biology >A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity.
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A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity.

机译：生长因子诱导的激酶在调节其DNA结合活性的位点使血清反应因子磷酸化。

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摘要

A signaling pathway by which growth factors may induce transcription of the c-fos proto-oncogene has been characterized. Growth factor stimulation of quiescent fibroblasts activates a protein kinase cascade that leads to the rapid and transient phosphorylation of the serum response factor (SRF), a regulator of c-fos transcription. The in vivo kinetics of SRF phosphorylation and dephosphorylation parallel the activation and subsequent repression of c-fos transcription, suggesting that this phosphorylation event plays a critical role in the control of c-fos expression. The ribosomal S6 kinase pp90rsk, a growth factor-inducible kinase, phosphorylates SRF in vitro at serine 103, the site that becomes newly phosphorylated upon growth factor stimulation in vivo. Phosphorylation of serine 103 significantly enhances the affinity and rate with which SRF associates with its binding site, the serum response element, within the c-fos promoter. These results suggest a model in which the growth factor-induced phosphorylation of SRF at serine 103 contributes to the activation of c-fos transcription by facilitating the formation of an active transcription complex at the serum response element.
机译：已经描述了生长因子可以诱导c-fos原癌基因转录的信号传导途径。静态成纤维细胞的生长因子刺激可激活蛋白激酶级联反应，从而导致血清反应因子（SRF）（c-fos转录的调节剂）快速而短暂地磷酸化。 SRF磷酸化和去磷酸化的体内动力学与c-fos转录的激活和随后的抑制平行，这表明该磷酸化事件在c-fos表达的控制中起关键作用。核糖体S6激酶pp90rsk（一种生长因子诱导性激酶）在体外在丝氨酸103处磷酸化SRF，该位点在体内被生长因子刺激后被新磷酸化。丝氨酸103的磷酸化显着提高了SRF与其在c-fos启动子内的结合位点，血清反应元件结合的亲和力和速率。这些结果提示了一种模型，其中通过促进血清反应元件上活性转录复合物的形成，丝氨酸103上的生长因子诱导的SRF磷酸化有助于c-fos转录的激活。

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