Biochemie-Zentrum der Universität Heidelberg, D-69120 Heidelberg, Germany.
J Cell Biol. 2011 Oct 17;195(2):183-92. doi: 10.1083/jcb.201105042. Epub 2011 Oct 10.
Unraveling the organization of the FG repeat meshwork that forms the active transport channel of the nuclear pore complex (NPC) is key to understanding the mechanism of nucleocytoplasmic transport. In this paper, we develop a tool to probe the FG repeat network in living cells by modifying FG nucleoporins (Nups) with a binding motif (engineered dynein light chain-interacting domain) that can drag several copies of an interfering protein, Dyn2, into the FG network to plug the pore and stop nucleocytoplasmic transport. Our method allows us to specifically probe FG Nups in vivo, which provides insight into the organization and function of the NPC transport channel.
阐明形成核孔复合物（NPC）主动转运通道的 FG 重复网格的组织方式是理解核质转运机制的关键。在本文中，我们通过修饰 FG 核孔蛋白（Nups）来开发一种在活细胞中探测 FG 重复网络的工具，该工具带有一个结合基序（工程化的动力蛋白轻链相互作用结构域），可以将几个干扰蛋白 Dyn2 拖入 FG 网络中，堵塞核孔并阻止核质转运。我们的方法允许我们在体内特异性地探测 FG Nups，这为 NPC 转运通道的组织和功能提供了深入的了解。
