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首页> 外文期刊>Journal of Molecular Biology >Phosphorylation of USP15 and USP4 Regulates Localization and Spliceosomal Deubiquitination
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Phosphorylation of USP15 and USP4 Regulates Localization and Spliceosomal Deubiquitination

机译：USP15和USP4的磷酸化调节本地化和抗乳糖体脱氮

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Deubiquitinating enzymes have key roles in diverse cellular processes whose enzymatic activities are regulated by different mechanisms including post-translational modification. Here, we show that USP15 is phosphorylated, and its localization and activity are dependent on the phosphorylation status. Nuclear-cytoplasmic fractionation and mass spectrometric analysis revealed that Thr149 and Thr219 of human USP15, which is conserved among different species, are phosphorylated in the cytoplasm. The phosphorylation status of USP15 at these two positions alters the interaction with its partner protein SART3, consequently leading to its nuclear localization and deubiquitinating activity toward the substrate PRP31. Treatment of cells with purvalanol A, a cyclin-dependent kinase inhibitor, results in nuclear translocation of USP15. USP4, another deubiquitinating enzyme with a high sequence homology and domain structure as USP15, also showed purvalanol A-dependent changes in activity and localization. Collectively, our data suggest that modifications of USP15 and USP4 by phosphorylation are important for the regulation of their localization required for cellular function in the spliceosome. (C) 2019 Published by Elsevier Ltd.
机译：脱硫酶在不同的细胞过程中具有关键作用，其酶活性由包括翻译后修饰的不同机制调节。在这里，我们表明USP15是磷酸化的，其本地化和活性取决于磷酸化状态。核 - 细胞质分级和质谱分析显示，在不同物种中保守的人USP15的THR149和THR219在细胞质中磷酸化。 USP15在这两个位置的磷酸化状态改变了与其伴侣蛋白SART3的相互作用，从而导致其核定位和脱水活性朝向基质PRP31。用purvalanol A治疗细胞，系蛋白依赖性激酶抑制剂，导致USP15的核易位。 USP4，另一种具有高序列同源性和域结构作为USP15的脱氮酶，还显示出普赖瓦醇依赖于活性和定位的变化。集体，我们的数据表明USP15和USP4通过磷酸化的修饰对于调节其定位对抗乳头组细胞功能所需的定位是重要的。 （c）2019年由elestvier有限公司发布

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