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首页> 外文期刊>Molecular and Cellular Biology >Differential Phosphorylation Controls Maskin Association with Eukaryotic Translation Initiation Factor 4E and Localization on the Mitotic Apparatus
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Differential Phosphorylation Controls Maskin Association with Eukaryotic Translation Initiation Factor 4E and Localization on the Mitotic Apparatus

机译：差异磷酸化控制Maskin与真核翻译起始因子4E和有丝分裂设备上的本地化的关联。

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Several cytoplasmic polyadenylation element (CPE)-containing mRNAs that are repressed in Xenopus oocytes become active during meiotic maturation. A group of factors that are anchored to the CPE are responsible for this repression and activation. Two of the most important are CPEB, which binds directly to the CPE, and Maskin, which associates with CPEB. In oocytes, Maskin also binds eukaryotic translation initiation factor 4E (eIF4E), an interaction that excludes eIF4G and prevents formation of the eIF4F initiation complex. When the oocytes are stimulated to reenter the meiotic divisions (maturation), CPEB promotes cytoplasmic polyadenylation. The newly elongated poly(A) tail becomes bound by poly(A) binding protein (PABP), which in turn binds eIF4G and helps it displace Maskin from eIF4E, thereby inducing translation. Here we show that Maskin undergoes several phosphorylation events during oocyte maturation, some of which are important for its dissociation from eIF4E and translational activation of CPE-containing mRNA. These sites are T58, S152, S311, S343, S453, and S638 and are phosphorylated by cdk1. Mutation of these sites to alanine alleviates the cdk1-induced dissociation of Maskin from eIF4E. Prior to maturation, Maskin is phosphorylated on S626 by protein kinase A. While this modification has no detectable effect on translation during oocyte maturation, it is critical for this protein to localize on the mitotic apparatus in somatic cells. These results show that Maskin activity and localization is controlled by differential phosphorylation.
机译：在非洲爪蟾卵母细胞中受阻的几个含胞质聚腺苷酸化元件（CPE）的mRNA在减数分裂成熟过程中变得活跃。固定在CPE上的一组因素负责这种抑制和激活。其中最重要的两个是CPEB（直接与CPE结合）和Maskin（与CPEB关联）。在卵母细胞中，Maskin也结合真核翻译起始因子4E（eIF4E），这种相互作用排除了eIF4G并阻止了eIF4F起始复合物的形成。当刺激卵母细胞重新进入减数分裂（成熟）时，CPEB促进细胞质聚腺苷酸化。新拉长的poly（A）尾巴被poly（A）结合蛋白（PABP）结合，后者又结合了eIF4G，并帮助其从eIF4E置换了Maskin，从而诱导翻译。在这里，我们显示Maskin在卵母细胞成熟过程中经历了几次磷酸化作用，其中一些对于其与eIF4E的解离和含CPE的mRNA的翻译激活非常重要。这些位点是T58，S152，S311，S343，S453和S638，并被cdk1磷酸化。这些位点突变为丙氨酸可减轻cdk1诱导的Maskin从eIF4E的解离。在成熟之前，Maskin被蛋白激酶A磷酸化在S626上。尽管这种修饰对卵母细胞成熟过程中的翻译没有可检测到的影响，但对于这种蛋白而言，在体细胞中定位在有丝分裂装置上至关重要。这些结果表明，掩模素活性和定位受差异磷酸化作用的控制。

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