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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160 subcomplex
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Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160 subcomplex

机译：Nup107-160亚复合物核孔的细胞周期依赖性磷酸化

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The nuclear pore complex (NPC) mediates macromolecular transport between the nucleus and the cytoplasm. Many NPC proteins (nucleoporins, Nups) are modified by phosphorylation. It is believed that phosphorylation regulates the breakdown of the nuclear envelope at mitosis and the disassembly of the NPC into different subcomplexes. In this study, we examined the cell-cycle-dependent phosphorylation of the Nup107-160 subcomplex, a core building block of the NPC. Using in vivo ~(32)P labeling in HeLa cells, we found that Nup107, Nup96, and Nup133 are phosphorylated during mitosis. To precisely map the phosphorylation sites within the complex, we used a comprehensive multiple-stage MS approach (MS, MS~2, and MS~3), establishing that Nup160, Nup133, Nup96, and Nup107 are all targets of phosphorylation. We determined that the phosphorylation sites are clustered mainly at the N-terminal regions of these proteins, which are predicted to be natively disordered. In addition, we determined the cell-cycle dependence of the phosphorylation of these sites by using stable isotope labeling and MS~2 analysis. Measurement of the site-specific phosphorylation ratios between mitotic and G_1 cells led us to conclude that several phosphorylation events of the subcomplex are mainly mitotic. Based on these results and our finding that the entire Nup107-160 subcomplex is stable throughout the cell cycle, we propose that phosphorylation does not affect interactions within the Nup107-160 subcomplex, but regulates the association of the subcomplex with the NPC and other proteins.
机译：核孔复合体（NPC）介导细胞核与细胞质之间的大分子转运。许多NPC蛋白（核孔蛋白，Nups）被磷酸化修饰。据信磷酸化调节有丝分裂时核被膜的分解和将NPC分解成不同的亚复合物。在这项研究中，我们检查了Nup107-160亚复合物（NPC的核心组成部分）的细胞周期依赖性磷酸化。在HeLa细胞中使用体内〜（32）P标记，我们发现Nup107，Nup96和Nup133在有丝分裂过程中被磷酸化。为了精确定位复合物中的磷酸化位点，我们使用了一种全面的多阶段MS方法（MS，MS〜2和MS〜3），确定Nup160，Nup133，Nup96和Nup107都是磷酸化的目标。我们确定磷酸化位点主要聚集在这些蛋白质的N端区域，预计是天然无序的。此外，我们通过使用稳定同位素标记和MS〜2分析确定了这些位点磷酸化的细胞周期依赖性。测量有丝分裂和G_1细胞之间的位点特异性磷酸化比率可以得出结论，亚复合体的一些磷酸化事件主要是有丝分裂。根据这些结果和我们的发现，即整个Nup107-160亚复合物在整个细胞周期中都是稳定的，我们提出磷酸化作用不会影响Nup107-160亚复合物之间的相互作用，但会调节该亚复合物与NPC和其他蛋白质的缔合。

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