Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, Netherlands Proteomics Centre, Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, Netherlands.
Science. 2011 Jul 1;333(6038):90-3. doi: 10.1126/science.1205741. Epub 2011 Jun 9.
Active nuclear import of soluble cargo involves transport factors that shuttle cargo through the nuclear pore complex (NPC) by binding to phenylalanine-glycine (FG) domains. How nuclear membrane proteins cross through the NPC to reach the inner membrane is presently unclear. We found that at least a 120-residue-long intrinsically disordered linker was required for the import of membrane proteins carrying a nuclear localization signal for the transport factor karyopherin-α. We propose an import mechanism for membrane proteins in which an unfolded linker slices through the NPC scaffold to enable binding between the transport factor and the FG domains in the center of the NPC.
可溶性货物的主动核输入涉及穿梭运输因子，这些因子通过与苯丙氨酸-甘氨酸（FG）结构域结合将货物穿梭过核孔复合体（NPC）。目前尚不清楚核膜蛋白如何穿过 NPC 到达内膜。我们发现，对于携带核定位信号的运输因子亲核蛋白-α的膜蛋白的输入，至少需要一个 120 个残基长的固有无序连接子。我们提出了一种膜蛋白的输入机制，其中未折叠的连接子穿过 NPC 支架，从而使运输因子与 NPC 中心的 FG 结构域之间能够结合。
