ISG15 modification of the eIF4E cognate 4EHP enhances cap structure-binding activity of 4EHP
ISG15 modification of the eIF4E cognate 4EHP enhances cap structure-binding activity of 4EHP
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DOI：
10.1101/gad.1521607
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发表时间：
2007-02-01
影响因子：
10.5
通讯作者：
Zhang, Dong-Er
中科院分区：
文献类型：
--
作者：
Okumura, Fumihiko;Zou, Weiguo;Zhang, Dong-Er
泛素样分子ISG15的表达和通过ISG15的蛋白质修饰（ISGylation）被干扰素、基因毒性应激和病原体感染强烈激活，表明ISG15在先天免疫应答中起重要作用。4EHP是mRNA 5'帽结构结合蛋白，通过与eIF4E竞争结合帽结构而充当翻译抑制因子。在这里，我们报告4EHP被ISG15修饰，ISG15修饰的4EHP具有更高的帽结构结合活性。这些数据表明，4EHP的ISG化可能在免疫应答中的帽结构依赖性翻译控制中起重要作用。
The expression of the ubiquitin-like molecule ISG15 and protein modification by ISG15 (ISGylation) are strongly activated by interferon, genotoxic stress, and pathogen infection, suggesting that ISG15 plays an important role in innate immune responses. 4EHP is an mRNA 5' cap structure-binding protein and acts as a translation suppressor by competing with eIF4E for binding to the cap structure. Here, we report that 4EHP is modified by ISG15 and ISGylated 4EHP has a much higher cap structure-binding activity. These data suggest that ISGylation of 4EHP may play an important role in cap structure-dependent translation control in immune responses.