Mansfeld Jörg, Güttinger Stephan, Hawryluk-Gara Lisa A, Panté Nelly, Mall Moritz, Galy Vincent, Haselmann Uta, Mühlhäusser Petra, Wozniak Richard W, Mattaj Iain W, Kutay Ulrike, Antonin Wolfram
Institute of Biochemistry, ETH Zurich, CH-8093 Zurich, Switzerland.
Mol Cell. 2006 Apr 7;22(1):93-103. doi: 10.1016/j.molcel.2006.02.015.
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.
核孔复合体（NPCs）是嵌入核膜（NE）的大型蛋白质通道，通过这些通道，细胞核与细胞质之间发生分子交换。NPCs的生物发生过程复杂，目前了解甚少。特别是，关于NPCs如何锚定在核膜上几乎一无所知。在这里，我们对脊椎动物NDC1进行了表征，NDC1是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）和生化去除实验表明，NDC1在体内和体外的NPC和核膜组装中发挥重要作用。RNAi实验表明NDC1与可溶性核孔蛋白Nup93、Nup53和Nup205之间存在功能联系。重要的是，NDC1在体外与Nup53相互作用。这表明NDC1的功能涉及在核膜和可溶性核孔蛋白之间形成连接，从而将NPC锚定在膜上。
