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首页> 外文期刊>Molecular and Cellular Biology >Akt-Mediated YB-1 Phosphorylation Activates Translation of Silent mRNA Species
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Akt-Mediated YB-1 Phosphorylation Activates Translation of Silent mRNA Species

机译：Akt介导的YB-1磷酸化激活沉默的mRNA物种的翻译。

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YB-1 is a broad-specificity RNA-binding protein that is involved in regulation of mRNA transcription, splicing, translation, and stability. In both germinal and somatic cells, YB-1 and related proteins are major components of translationally inactive messenger ribonucleoprotein particles (mRNPs) and are mainly responsible for storage of mRNAs in a silent state. However, mechanisms regulating the repressor activity of YB-1 are not well understood. Here we demonstrate that association of YB-1 with the capped 5′ terminus of the mRNA is regulated via phosphorylation by the serine/threonine protein kinase Akt. In contrast to its nonphosphorylated form, phosphorylated YB-1 fails to inhibit cap-dependent but not internal ribosome entry site-dependent translation of a reporter mRNA in vitro. We also show that similar to YB-1, Akt is associated with inactive mRNPs and that activated Akt may relieve translational repression of the YB-1-bound mRNAs. Using Affymetrix microarrays, we found that many of the YB-1-associated messages encode stress- and growth-related proteins, raising the intriguing possibility that Akt-mediated YB-1 phosphorylation could, in part, increase production of proteins regulating cell proliferation, oncogenic transformation, and stress response.
机译：YB-1是一种广泛特异性的RNA结合蛋白，参与mRNA转录，剪接，翻译和稳定性的调控。在生殖细胞和体细胞中，YB-1和相关蛋白都是翻译不活跃的信使核糖核蛋白颗粒（mRNPs）的主要成分，并且主要负责沉默状态下mRNA的存储。但是，尚不清楚调节YB-1阻遏物活性的机制。在这里，我们证明了丝氨酸/苏氨酸蛋白激酶Akt通过磷酸化来调节YB-1与mRNA的5'端的结合。与它的非磷酸化形式相反，磷酸化的YB-1在体外不能抑制报道分子mRNA的帽依赖性翻译，而不能抑制内部核糖体进入位点依赖性翻译。我们还表明，类似于YB-1，Akt与非活性mRNPs相关，而活化的Akt可能减轻YB-1结合mRNA的翻译抑制。使用Affymetrix微阵列，我们发现许多与YB-1相关的信息均编码与压力和生长相关的蛋白质，从而增加了Akt介导的YB-1磷酸化可以部分增加调节细胞增殖的蛋白质的产生的有趣可能性，致癌转化和应激反应。

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