• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Nucleus >Mitotic phosphorylation of SUN1 loosens its connection with the nuclear lamina while the LINC complex remains intact
【24h】

Mitotic phosphorylation of SUN1 loosens its connection with the nuclear lamina while the LINC complex remains intact

机译：SUN1的有丝分裂磷酸化可放松其与核层的连接，而LINC复合物仍保持完整

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

At the onset mitosis in higher eukaryotes, the nuclear envelope (NE) undergoes dramatic deconstruction to allow separation of duplicated chromosomes. Studies have shown that during this process of nuclear envelope breakdown (NEBD), the extensive protein networks of the nuclear lamina are disassembled through phosphorylation of lamins and several inner nuclear membrane (INM) proteins. The LINC complex, composed of SUN and nesprin proteins, is involved in multiple interactions at the NE and plays vital roles in nuclear and cellular mechanics by connecting the nucleus to the cytoskeleton. Here, we show that SUN1, located in the INM, undergoes mitosis-specific phosphorylation on at least 3 sites within its nucleoplasmic N-terminus. We further identify Cdk1 as the kinase responsible for serine 48 and 333 phosphorylation, while serine 138 is phosphorylated by Plk1. In mitotic cells, SUN1 loses its interaction with N-terminal domain binding partners lamin A/C, emerin, and short nesprin-2 isoforms. Furthermore, a triple phosphomimetic SUN1 mutant displays increased solubility and reduced retention at the NE. In contrast, the central LINC complex interaction between the SUN1 C-terminus and the KASH domain of nesprin-2 is maintained during mitosis. Together, these data support a model whereby mitotic phosphorylation of SUN1 disrupts interactions with nucleoplasmic binding partners, promoting disassembly of the nuclear lamina and, potentially, its chromatin interactions. At the same time, our data add to an emerging picture that the core LINC complex plays an active role in NEBD.
机译：在高等真核生物的有丝分裂开始时，核被膜（NE）经历了巨大的解构，从而可以分离出重复的染色体。研究表明，在核被膜破裂（NEBD）的过程中，核纤层蛋白的广泛蛋白质网络通过核纤层蛋白和几种内核膜（INM）蛋白的磷酸化而分解。由SUN和雀巢蛋白组成的LINC复合物在NE参与多种相互作用，并通过将核连接到细胞骨架在核和细胞力学中发挥重要作用。在这里，我们表明，位于INM的SUN1在其核质N端的至少3个位点经历有丝分裂特异性磷酸化。我们进一步确定Cdk1为负责丝氨酸48和333磷酸化的激酶，而丝氨酸138被Plk1磷酸化。在有丝分裂细胞中，SUN1失去了与N末端域结合伴侣lamin A / C，emerin和短nesprin-2亚型的相互作用。此外，三磷酸拟SUN1突变体显示增加的溶解度和减少保留在NE。相反，在有丝分裂过程中，SUN1 C末端与nesprin-2的KASH域之间的中央LINC复合体相互作用得以维持。总之，这些数据支持了一个模型，在该模型中，SUN1的有丝分裂磷酸化破坏了与核质结合伴侣的相互作用，从而促进了核纤层的分解，并可能促进了其染色质的相互作用。同时，我们的数据增加了一个新的印象，即核心LINC复合体在NEBD中起着积极的作用。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号