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Regulation of nuclear envelope breakdown by the nuclear pore complex

机译：核孔复合体对核被膜破坏的调控

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摘要

In higher eukaryotes, each time a cell divides dramatic changes occur at the nuclear periphery. The nuclear envelope, nuclear pore complexes, and nuclear lamina must disassemble to allow the mitotic spindle access to the genomic DNA, but little is known about the mechanisms required for these breakdown events. In order to biochemically dissect these events, we have optimized an assay to study nuclear disassembly in vitro using Xenopus egg extracts. One of the early events in nuclear envelope breakdown is disassembly of the nuclear pore complexes suggesting that the nuclear pores may be an important organizing center of mitotic events. We have identified a role for two nuclear pore proteins, Nup153 and Nup358/RanBP2, in recruiting the COPI coatomer complex to the nuclear envelope during nuclear disassembly. Adding antibody specific to either of these nuclear pore proteins individually inhibits nuclear disassembly, suggesting the nucleoporins are required in a nonredundant manner. The zinc finger domains within these nucleoporins appear to be the critical determinants for their role in nuclear envelope breakdown, since addition of recombinant zinc finger fragments derived from either pore protein alters COPI recruitment to the nuclear envelope and interferes with nuclear envelope breakdown. The localization of Nup153 and Nup358 to the nuclear basket and cytoplasmic filaments of the nuclear pore, respectively, suggests that recruitment of COPI to both faces of the pore is important. The COPI complex is known to have a role in vesicle trafficking from the Golgi to the ER and may play a similar role at the nuclear envelope during disassembly. The zinc finger fragments also prevent disassembly of the nuclear lamina, suggesting that recruitment of COPI to the nuclear envelope may be critical for coordinating dispersal of the membrane with other cell cycle events.;Nuclei disassembled during prophase must then be efficiently reassembled during anaphase. Using dominant negative recombinant protein fragments, we have found that Nup153 interacts with regulators required for nuclear assembly and DNA replication. These results provide new information about the critical components of nuclear assembly and disassembly and lay the foundation for a better understanding of how these processes are regulated.
机译：在高等真核生物中，每次细胞分裂都会在核外围发生剧烈变化。核被膜，核孔复合物和核层必须分解才能使有丝分裂纺锤体进入基因组DNA，但对于这些分解事件所需的机制知之甚少。为了对这些事件进行生物化学分析，我们优化了一种使用非洲爪蟾卵提取物体外研究核分解的方法。核被膜破裂的早期事件之一是核孔复合物的分解，表明核孔可能是有丝分裂事件的重要组织中心。我们已经确定了两个核孔蛋白Nup153和Nup358 / RanBP2在核拆卸过程中将COPI涂层复合物募集到核膜中的作用。添加对这些核孔蛋白中的任一个特异性的抗体会分别抑制核解体，表明核孔蛋白是非冗余方式所必需的。这些核孔蛋白中的锌指结构域似乎是它们在核被膜破裂中发挥作用的关键决定因素，因为添加衍生自任一孔蛋白的重组锌指片段会改变COPI募集到核被膜并干扰核被膜破裂。 Nup153和Nup358分别定位于核孔的核篮和细胞质细丝，这表明将COPI募集到孔的两面很重要。已知COPI复合物在从高尔基体到内质网的小泡运输中起作用，并且在拆卸过程中可能在核膜上起类似作用。锌指碎片还可以防止核层的解体，这表明将COPI募集到核膜可能对于协调膜的扩散与其他细胞周期事件至关重要。;在前期解体的核子必须在后期进行有效的重组。使用显性阴性重组蛋白片段，我们发现Nup153与核装配和DNA复制所需的调节子相互作用。这些结果提供了有关核组装和拆卸的关键组成部分的新信息，并为更好地了解如何调节这些过程奠定了基础。

著录项

  • 作者

    Prunuske, Amy Jeannette.;

  • 作者单位

    The University of Utah.;

  • 授予单位 The University of Utah.;
  • 学科 Molecular biology.
  • 学位 Ph.D.
  • 年度 2006
  • 页码 130 p.
  • 总页数 130
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

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