Ksp1-dependent phosphorylation of eIF4G modulates post-transcriptional regulation of specific mRNAs under glucose deprivation conditions.
Ksp1-dependent phosphorylation of eIF4G modulates post-transcriptional regulation of specific mRNAs under glucose deprivation conditions.
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DOI：
10.1093/nar/gky097
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发表时间：
2018-04-06
影响因子：
14.9
通讯作者：
Huh WK
中科院分区：
文献类型：
--
作者：
Chang Y;Huh WK
转录后调节是调节基因表达的重要机制，由许多mRNA结合蛋白进行。为了了解转录后调控的机制，我们研究了葡萄糖剥夺条件下酿酒酵母中32个mRNA结合蛋白的磷酸化状态。我们确定了17个葡萄糖敏感磷蛋白和信号通路参与其磷酸化。值得注意的是，真核生物翻译起始因子4G（eIF 4G）的磷酸化受Snf 1/AMPK途径和雷帕霉素复合物1（TORC 1）靶点途径的调节。丝氨酸/苏氨酸蛋白激酶Ksp 1以前被认为是TORC 1的下游效应子，但其详细功能很少被讨论。我们发现，Snf 1/AMPK和TORC 1信号收敛于Ksp 1，在葡萄糖剥夺条件下磷酸化eIF 4G。在葡萄糖剥夺条件下，eIF 4G的Ksp 1依赖性磷酸化调节特定mRNA（例如糖酵解mRNA和核糖体蛋白mRNA）的降解，可能是通过募集Dhh 1。两者合计，我们的研究结果表明，Ksp 1功能作为一种新的调制器的转录后调控酵母。
Post-transcriptional regulation is an important mechanism for modulating gene expression and is performed by numerous mRNA-binding proteins. To understand the mechanisms underlying post-transcriptional regulation, we investigated the phosphorylation status of 32 mRNA-binding proteins under glucose deprivation conditions in Saccharomyces cerevisiae. We identified 17 glucose-sensitive phosphoproteins and signal pathways implicated in their phosphorylation. Notably, phosphorylation of the eukaryotic translation initiation factor 4G (eIF4G) was regulated by both the Snf1/AMPK pathway and the target of rapamycin complex 1 (TORC1) pathway. The serine/threonine protein kinase Ksp1 has previously been suggested to be a downstream effector of TORC1, but its detailed function has rarely been discussed. We identified that Snf1/AMPK and TORC1 signalings converge on Ksp1, which phosphorylates eIF4G under glucose deprivation conditions. Ksp1-dependent phosphorylation of eIF4G regulates the degradation of specific mRNAs (e.g. glycolytic mRNAs and ribosomal protein mRNAs) under glucose deprivation conditions likely through the recruitment of Dhh1. Taken together, our results suggest that Ksp1 functions as a novel modulator of post-transcriptional regulation in yeast.
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