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首页> 外文期刊>Molecular and Cellular Biology >OGFOD1, a Novel Modulator of Eukaryotic Translation Initiation Factor 2α Phosphorylation and the Cellular Response to Stress
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OGFOD1, a Novel Modulator of Eukaryotic Translation Initiation Factor 2α Phosphorylation and the Cellular Response to Stress

机译：OGFOD1，新型的真核翻译起始因子2α磷酸化调节剂和细胞对应激的反应

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Cells possess mechanisms that permit survival and recovery from stress, several of which regulate the phosphorylation of eukaryotic translation initiation factor 2α (eIF2α). We identified the human OGFOD1 protein as a novel stress granule component that regulates the phosphorylation of eIF2α and the resumption of translation in cells recovering from arsenite-induced stress. Coimmunoprecipitation studies revealed that OGFOD1 associates with a small subset of stress granule proteins (G3BP1, USP10, Caprin1, and YB-1) and the ribosome in both unstressed and stressed cells. Overexpression of OGFOD1 led to increased abundance of phosphorylated eIF2α, both in unstressed cells and in cells exposed to arsenite-induced stress, and to accelerated apoptosis during stress. Conversely, knockdown of OGFOD1 resulted in smaller amounts of phosphorylated eIF2α and a faster accumulation of polyribosomes in cells recovering from stress. Finally, OGFOD1 interacted with both eIF2α and the eIF2α kinase heme-regulated inhibitor (HRI), which was identified as a novel stress granule resident. These findings argue that OGFOD1 plays important proapoptotic roles in the regulation of translation and HRI-mediated phosphorylation of eIF2α in cells subjected to arsenite-induced stress.
机译：细胞具有允许在压力下存活和恢复的机制，其中一些机制可调节真核翻译起始因子2α（eIF2α）的磷酸化。我们确定了人类OGFOD1蛋白是一种新型的应激颗粒成分，可调节eIF2α的磷酸化以及从亚砷酸盐诱导的应激中恢复细胞的翻译恢复。免疫共沉淀研究表明，OGFOD1与一小部分应激颗粒蛋白（G3BP1，USP10，Caprin1和YB-1）和核糖体在无应激和应激细胞中缔合。 OGFOD1的过表达导致未应激细胞和暴露于砷诱导的应激的细胞中磷酸化eIF2α的丰度增加，并导致应激期间的细胞凋亡加速。相反，敲除OGFOD1可使磷酸化的eIF2α含量降低，而多核糖体在压力下恢复的速度更快。最后，OGFOD1与eIF2α和eIF2α激酶血红素调节抑制剂（HRI）相互作用，这被确定为一种新型的应激颗粒。这些发现表明，OGFOD1在受砷诱导的细胞中的翻译和HRI介导的eIF2α磷酸化的调节中起着重要的促凋亡作用。

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