The conserved transmembrane nucleoporin NDC1 is required for nuclear pore complex assembly in vertebrate cells
The conserved transmembrane nucleoporin NDC1 is required for nuclear pore complex assembly in vertebrate cells
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DOI：
10.1016/j.molcel.2006.02.015
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发表时间：
2006-04-07
期刊：
影响因子：
16
通讯作者：
Antonin, W
中科院分区：
文献类型：
--
作者：
Mansfeld, J;Güttinger, S;Antonin, W
核孔复合物（Nuclear pore complex，NPC）是一种嵌入核膜（Nuclear envelope，NE）中的蛋白质通道，细胞核与胞质之间通过它进行分子交换。NPC的生物发生是复杂的，并且知之甚少。特别是，几乎没有人知道NPC是如何锚定在NE中的。在这里，我们表征脊椎动物NDC 1-酵母和后生动物之间保守的跨膜核孔蛋白。我们通过RNA干扰（RNAi）和生化耗竭表明，NDC 1在体内和体外NPC和NE组装中起着重要作用。RNAi实验表明NDC 1与可溶性核孔蛋白Nup 93、Nup 53和Nup 205之间存在功能性联系。重要的是，NDC 1在体外与Nup 53相互作用。这表明NDC 1功能涉及在NE膜和可溶性核孔蛋白之间形成连接，从而将NPC锚定在膜中。
Nuclear pore complexes (NPCs) are large proteinaceous channels embedded in the nuclear envelope (NE), through which exchange of molecules between the nucleus and cytosol occurs. Biogenesis of NPCs is complex and poorly understood. In particular, almost nothing is known about how NPCs are anchored in the NE. Here, we characterize vertebrate NDC1-a transmembrane nucleoporin conserved between yeast and metazoans. We show by RNA interference (RNAi) and biochemical depletion that NDC1 plays an important role in NPC and NE assembly in vivo and in vitro. RNAi experiments suggest a functional link between NDC1 and the soluble nucleoporins Nup93, Nup53, and Nup205. Importantly, NDC1 interacts with Nup53 in vitro. This suggests that NDC1 function involves forming a link between the NE membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane.