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COPI复合体在核膜破裂过程中发挥作用,并由核孔蛋白Nup153招募。

The COPI complex functions in nuclear envelope breakdown and is recruited by the nucleoporin Nup153.

作者信息

Liu Jin, Prunuske Amy J, Fager Ammon M, Ullman Katharine S

机构信息

Department of Oncological Sciences, Huntsman Cancer Institute, 2000 Circle of Hope, University of Utah, Salt Lake City, UT 84112, USA.

出版信息

Dev Cell. 2003 Sep;5(3):487-98. doi: 10.1016/s1534-5807(03)00262-4.

Abstract

Nuclear envelope breakdown is a critical step in the cell cycle of higher eukaryotes. Although integral membrane proteins associated with the nuclear membrane have been observed to disperse into the endoplasmic reticulum at mitosis, the mechanisms involved in this reorganization remain to be fully elucidated. Here, using Xenopus extracts, we report a role for the COPI coatomer complex in nuclear envelope breakdown, implicating vesiculation as an important step. We have found that a nuclear pore protein, Nup153, plays a critical role in directing COPI to the nuclear membrane at mitosis and that this event provides feedback to other aspects of nuclear disassembly. These results provide insight into how key steps in nuclear division are orchestrated.

摘要

核膜破裂是高等真核生物细胞周期中的关键步骤。尽管已观察到与核膜相关的整合膜蛋白在有丝分裂时会分散到内质网中,但这种重组所涉及的机制仍有待充分阐明。在此,我们利用非洲爪蟾提取物报告了COP I衣被蛋白复合体在核膜破裂中的作用,表明囊泡形成是一个重要步骤。我们发现一种核孔蛋白Nup153在有丝分裂时将COP I引导至核膜的过程中起关键作用,并且这一事件会反馈到核解体的其他方面。这些结果为核分裂关键步骤的协调机制提供了见解。

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