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Modulation of an RNA-binding protein by abscisic-acid-activated protein kinase

机译:脱落酸激活蛋白激酶对RNA结合蛋白的调节

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Protein kinases are involved in stress signalling in both plant and animal systems. The hormone abscisic acid mediates the responses of plants to stresses such as drought, salinity and cold. Abscisic-acid-activated protein kinase (AAPK)― found in guard cells, which control stomatal pores― has been shown to regulate plasma membrane ion channels. Here we show that AAPK―interacting protein 1 (AKIP1), with sequence homology to heterogeneous nuclear RNA-binding protein A/B, is a substrate of AAPK. APK-dependent phosphorylation is required for the interaction of AKIP1 with messenger RNA that encodes dehy-drin, a protein implicated in cell protection under stress conditions. AAPK and AKIP1 are present in the guard-cell nucleus, and in vivo treatment of such cells with abscisic acid enhances the partitioning of AKIP1 into subnuclear foci which are reminiscent of nuclear speckles. These results show that phosphorylation-regulated RNA target discrimination by heterogeneous nuclcar RNA-binding proteins may be a general phenomenon in eukar-yotes, and implicate a plant hormone in the regulation of protein dynamics during rapid subnuclear reorganization.
机译:蛋白激酶参与植物和动物系统的应激信号传递。脱落酸激素介导植物对干旱,盐碱和寒冷等胁迫的反应。保卫细胞中存在的脱落酸激活蛋白激酶(AAPK)控制着气孔,已被证明可以调节质膜离子通道。在这里,我们显示与异质核RNA结合蛋白A / B具有序列同源性的AAPK相互作用蛋白1(AKIP1)是AAPK的底物。 AKIP1与编码脱氢蛋白的信使RNA相互作用需要APK依赖的磷酸化,脱氢蛋白是一种在应激条件下参与细胞保护的蛋白。 AAPK和AKIP1存在于保卫细胞核中,在体内用脱落酸处理此类细胞可增强AKIP1在亚核灶中的分配,这使人联想到核斑点。这些结果表明异核核糖RNA结合蛋白的磷酸化调节的RNA靶标识别可能是真核生物中的普遍现象,并且在快速亚核重组过程中暗示了植物激素对蛋白质动力学的调节。

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