• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Molecular and Cellular Biology >RanBP2/Nup358 Provides a Major Binding Site for NXF1-p15 Dimers at the Nuclear Pore Complex and Functions in Nuclear mRNA Export
【24h】

RanBP2/Nup358 Provides a Major Binding Site for NXF1-p15 Dimers at the Nuclear Pore Complex and Functions in Nuclear mRNA Export

机译：RanBP2 / Nup358在核孔复合体中为NXF1-p15二聚体提供了主要的结合位点，并在核mRNA输出中发挥了作用

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

摘要

Metazoan NXF1-p15 heterodimers promote the nuclear export of bulk mRNA across nuclear pore complexes (NPCs). In vitro, NXF1-p15 forms a stable complex with the nucleoporin RanBP2/Nup358, a component of the cytoplasmic filaments of the NPC, suggesting a role for this nucleoporin in mRNA export. We show that depletion of RanBP2 from Drosophila cells inhibits proliferation and mRNA export. Concomitantly, the localization of NXF1 at the NPC is strongly reduced and a significant fraction of this normally nuclear protein is detected in the cytoplasm. Under the same conditions, the steady-state subcellular localization of other nuclear or cytoplasmic proteins and CRM1-mediated protein export are not detectably affected, indicating that the release of NXF1 into the cytoplasm and the inhibition of mRNA export are not due to a general defect in NPC function. The specific role of RanBP2 in the recruitment of NXF1 to the NPC is highlighted by the observation that depletion of CAN/Nup214 also inhibits cell proliferation and mRNA export but does not affect NXF1 localization. Our results indicate that RanBP2 provides a major binding site for NXF1 at the cytoplasmic filaments of the NPC, thereby restricting its diffusion in the cytoplasm after NPC translocation. In RanBP2-depleted cells, NXF1 diffuses freely through the cytoplasm. Consequently, the nuclear levels of the protein decrease and export of bulk mRNA is impaired.
机译：后生NXF1-p15异二聚体促进整个mRNA跨核孔复合物（NPC）的核输出。在体外，NXF1-p15与核孔蛋白RanBP2 / Nup358（一种NPC细胞质细丝的成分）形成稳定的复合物，表明该核孔蛋白在mRNA输出中的作用。我们显示，从果蝇细胞中耗尽RanBP2可抑制增殖和mRNA输出。伴随地，NXF1在NPC上的定位大大降低，并且在细胞质中检测到该正常核蛋白的很大一部分。在相同条件下，其他核蛋白或胞质蛋白的稳态亚细胞定位和CRM1介导的蛋白输出不受可检测到的影响，这表明NXF1释放到细胞质中和对mRNA输出的抑制不是由于一般缺陷引起的在NPC功能中。 RanBP2在NXF1募集到NPC中的特定作用通过以下观察突显出来：CAN / Nup214的耗竭也抑制细胞增殖和mRNA输出，但不影响NXF1的定位。我们的结果表明，RanBP2在NPC的细胞质细丝上为NXF1提供了主要的结合位点，从而限制了NPC易位后NXF1在细胞质中的扩散。在贫RanBP2的细胞中，NXF1在细胞质中自由扩散。因此，蛋白质的核水平降低并且大量mRNA的输出受损。

著录项

相似文献

  • 外文文献
  • 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