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首页> 外文期刊>The Journal of biological chemistry >Histone arginine demethylase JMJD6 is linked to stress granule assembly through demethylation of the stress granule–nucleating protein G3BP1
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Histone arginine demethylase JMJD6 is linked to stress granule assembly through demethylation of the stress granule–nucleating protein G3BP1

机译：组蛋白精氨酸脱甲基酶JMJD6通过应力颗粒成核蛋白G3BP1的脱甲基作用与应力颗粒组装相关联

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摘要

Stress granules (SG) are membrane-less organelles that are condensates of stalled translation initiation complexes and mRNAs. SG formation is a cytoprotective response to environmental stress and results from protein interactions involving regions of low amino acid complexity and poorly defined post-translational modifications of SG components. Many RNA-binding proteins are methylated, and we previously demonstrated that the potent SG–nucleating protein G3BP1 is methylated by protein arginine methyltransferase 1 and 5 (PRMT1 and PRMT5). G3BP1 methylation represses SG formation and is reversible. Here we functionally link JMJD6 (Jumonji C domain-containing protein 6) to G3BP1 demethylation. Our findings reveal that JMJD6 is a novel SG component that interacts with G3BP1 complexes, and its expression reduces G3BP1 monomethylation and asymmetric dimethylation at three Arg residues. Knockdown of JMJD6 repressed SG formation and G3BP1 demethylation, but SG formation and G3BP1 demethylation were rescued with catalytically active but not mutant JMJD6. These results suggest that JMJD6 functions directly or indirectly as an arginine demethylase of G3BP1 that promotes SG formation.
机译：应激颗粒（SG）是无膜细胞器，是停滞的翻译起始复合物和mRNA的冷凝物。 SG的形成是对环境胁迫的细胞保护反应，是由蛋白质相互作用引起的，该相互作用涉及氨基酸复杂性低的区域以及SG组分的翻译后修饰修饰不明确。许多RNA结合蛋白被甲基化，并且我们先前证明了强大的SG成核蛋白G3BP1被精氨酸甲基转移酶1和5（PRMT1和PRMT5）甲基化。 G3BP1甲基化可抑制SG的形成，并且是可逆的。在这里，我们在功能上将JMJD6（含有Jumonji C域的蛋白6）连接到G3BP1去甲基化。我们的发现表明，JMJD6是与G3BP1复合物相互作用的新型SG组分，其表达减少了三个Arg残基处的G3BP1单甲基化和不对称二甲基化。击倒JMJD6抑制了SG的形成和G3BP1的去甲基化，但是SG的形成和G3BP1的去甲基化被具有催化活性的突变体JMJD6拯救了。这些结果表明，JMJD6直接或间接充当G3BP1的精氨酸脱甲基酶，促进SG的形成。

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