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首页> 外文期刊>Nucleus >LEM-4 promotes rapid dephosphorylation of BAF during mitotic exit
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LEM-4 promotes rapid dephosphorylation of BAF during mitotic exit

机译：LEM-4促进有丝分裂退出过程中BAF的快速去磷酸化

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The transitions between the successive cell cycle stages depend on reversible protein phosphorylation events. The phosphorylation state of every protein within a cell is strictly determined by spatiotemporally controlled kinase and phosphatase activities. Nuclear disassembly and reassembly during open mitosis in higher eukaryotic cells is one such process that is tightly regulated by the reversible phosphorylation of key proteins. However, little is known about the regulation of these mitotic events. In particular, although kinase function during entry into mitosis is better studied, very little is known about how proteins are dephosphorylated to allow nuclear reformation at the end of mitosis. We have identified LEM?4, a conserved protein of the nuclear envelope, as an essential coordinator of kinase and phosphatase activities during mitotic exit. Inhibition of VRK?1 kinase and promotion of a PP2A phosphatase complex by LEM?4 tightly regulate the phosphorylation state of BAF, an essential player of nuclear reformation at the end of mitosis. Here I offer extended comments on the contribution of LEM?4 in the regulation of protein phosphorylation and nuclear reformation.
机译：连续细胞周期阶段之间的过渡取决于可逆的蛋白质磷酸化事件。细胞内每种蛋白质的磷酸化状态均由时空控制的激酶和磷酸酶活性严格确定。在高等真核细胞的开放有丝分裂过程中，核的拆卸和重新组装就是这样一种过程，它受到关键蛋白可逆磷酸化的严格调控。但是，关于这些有丝分裂事件的调控知之甚少。尤其是，尽管对进入有丝分裂期间的激酶功能进行了更好的研究，但对蛋白质如何被去磷酸化以允许在有丝分裂结束时进行核重组的了解甚少。我们已经确定了核包膜的保守蛋白LEMα4是有丝分裂退出过程中激酶和磷酸酶活性的重要调节剂。 LEMα4抑制VRKβ1激酶并促进PP2A磷酸酶复合物紧密调节BAF的磷酸化状态，BAF是有丝分裂结束时核再形成的重要参与者。在这里，我对LEM？4在调节蛋白质磷酸化和核重整中的作用提供了广泛的意见。

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