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首页> 外文期刊>Molecular and Cellular Biology >Interaction between hnRNPA1 and IκBα Is Required for Maximal Activation of NF-κB-Dependent Transcription
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Interaction between hnRNPA1 and IκBα Is Required for Maximal Activation of NF-κB-Dependent Transcription

机译：hnRNPA1和IκBα之间的相互作用是最大程度激活NF-κB依赖性转录所必需的

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摘要

Transcriptional activation of NF-κB is mediated by signal-induced phosphorylation and degradation of its inhibitor, IκBα. NF-κB activation induces a rapid resynthesis of IκBα which is responsible for postinduction repression of transcription. Following resynthesis, IκBα translocates to the nucleus, removes template bound NF-κB, and exports NF-κB to the cytoplasm in a transcriptionally inactive form. Here we demonstrate that IκBα interacts directly with another nucleocytoplasmic shuttling protein, hnRNPA1, both in vivo and in vitro. This interaction requires one of the N-terminal RNA binding domains of hnRNPA1 and the C-terminal region of IκBα. Cells lacking hnRNPA1 are defective in NF-κB-dependent transcriptional activation, but the defect in these cells is complemented by ectopic expression of hnRNPA1. hnRNPA1 expression in these cells increased the amount of IκBα degradation, compared to that of the control cells, in response to activation by Epstein-Barr virus latent membrane protein 1. Thus in addition to regulating mRNA processing and transport, hnRNPA1 also contributes to the control of NF-κB-dependent transcription.
机译：NF-κB的转录激活是由信号诱导的磷酸化及其抑制剂IκBα降解介导的。 NF-κB的激活诱导了IκBα的快速再合成，这是诱导转录后抑制的原因。重新合成后，IκBα易位至细胞核，去除与模板结合的NF-κB，并以转录失活的形式将NF-κB输出到细胞质。在这里，我们证明了IκBα在体内和体外都直接与另一个核质穿梭蛋白hnRNPA1相互作用。这种相互作用需要hnRNPA1的N端RNA结合结构域之一和IκBα的C端区域。缺少hnRNPA1的细胞在NF-κB依赖性转录激活中存在缺陷，但是这些细胞中的缺陷被hnRNPA1的异位表达所弥补。与控制细胞相比，这些细胞中hnRNPA1的表达增加了IκBα的降解量，这是由于爱泼斯坦-巴尔病毒潜伏膜蛋白1的激活而引起的。因此，除了调节mRNA的加工和运输，hnRNPA1还有助于控制依赖NF-κB的转录。

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