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首页> 外文期刊>Molecular and Cellular Biology >Activation of Pre-mRNA Splicing by Human RNPS1 Is Regulated by CK2 Phosphorylation
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Activation of Pre-mRNA Splicing by Human RNPS1 Is Regulated by CK2 Phosphorylation

机译：人RNPS1的前mRNA剪接的激活受CK2磷酸化的调节。

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Human RNPS1 was originally characterized as a pre-mRNA splicing activator in vitro and was shown to regulate alternative splicing in vivo. RNPS1 was also identified as a protein component of the splicing-dependent mRNP complex, or exon-exon junction complex (EJC), and a role for RNPS1 in postsplicing processes has been proposed. Here we demonstrate that RNPS1 incorporates into active spliceosomes, enhances the formation of the ATP-dependent A complex, and promotes the generation of both intermediate and final spliced products. RNPS1 is phosphorylated in vivo and interacts with the CK2 (casein kinase II) protein kinase. Serine 53 (Ser-53) of RNPS1 was identified as the major phosphorylation site for CK2 in vitro, and the same site is also phosphorylated in vivo. The phosphorylation status of Ser-53 significantly affects splicing activation in vitro, but it does not perturb the nuclear localization of RNPS1. In vivo experiments indicated that the phosphorylation of RNPS1 at Ser-53 influences the efficiencies of both splicing and translation. We propose that RNPS1 is a splicing regulator whose activator function is controlled in part by CK2 phosphorylation.
机译：人RNPS1最初在体外被表征为前mRNA剪接激活剂，并被证明在体内可调控其他剪接。 RNPS1还被确定为剪接依赖性mRNP复合物或外显子-外显子连接复合物（EJC）的蛋白质成分，并且有人提出RNPS1在后剪接过程中的作用。在这里，我们证明RNPS1掺入活性剪接体中，增强了ATP依赖性A复合物的形成，并促进了中间和最终剪接产物的产生。 RNPS1在体内被磷酸化并与CK2（酪蛋白激酶II）蛋白激酶相互作用。 RNPS1的丝氨酸53（Ser-53）被确定为体外CK2的主要磷酸化位点，并且该位点在体内也被磷酸化。 Ser-53的磷酸化状态在体外显着影响剪接激活，但不会干扰RNPS1的核定位。体内实验表明，RNPS1在Ser-53处的磷酸化影响剪接和翻译的效率。我们建议RNPS1是一个剪接调节剂，其激活子功能部分受CK2磷酸化作用控制。

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