核孔复合体（NPCs）介导核浆和细胞质之间的物质交换，在核酸和蛋白质分离成它们所需的区域中发挥着关键作用。最近冷冻电镜和其他研究对NPC的静态结构已相对明确。核孔复合物孔道中动态成分的功能作用，苯丙氨酰-甘氨酰（FG）重复富集核孔蛋白质，由于我们对高度动态蛋白质系统的了解有限，不太清楚。这些蛋白质形成“有限浓缩物”，与核运输因子（NTRs）相互作用并浓缩NTRs，为载荷提供促进核质转运。FG重复和NTRs之间的非常快速的开关速率支持极快的促进转运，接近于细胞质中大分子扩散的速率，而没有特定相互作用的复合物被熵排斥，尽管有关运输机理和FG重复行为的几个方面的细节仍有待解决。然而，正如本文所讨论的，新的技术方法结合更先进的建模方法有可能在不久的将来提供更好的NPC运输动态描述，潜在地在原子水平上。这样的进步有可能在理解NPC功能失调在癌症、衰老、病毒性疾病和神经退行性疾病中所起的作用方面带来重大好处。©2023作者。

Nuclear pore complexes (NPCs) mediate the exchange of materials between the nucleoplasm and cytoplasm, playing a key role in the separation of nucleic acids and proteins into their required compartments. The static structure of the NPC is relatively well defined by recent cryo-EM and other studies. The functional roles of dynamic components in the pore of the NPC, phenylalanyl-glycyl (FG) repeat rich nucleoporins, is less clear because of our limited understanding of highly dynamic protein systems. These proteins form a 'restrained concentrate' which interacts with and concentrates nuclear transport factors (NTRs) to provide facilitated nucleocytoplasmic transport of cargoes. Very rapid on- and off-rates among FG repeats and NTRs supports extremely fast facilitated transport, close to the rate of macromolecular diffusion in cytoplasm, while complexes without specific interactions are entropically excluded, though details on several aspects of the transport mechanism and FG repeat behaviors remain to be resolved. However, as discussed here, new technical approaches combined with more advanced modeling methods will likely provide an improved dynamic description of NPC transport, potentially at the atomic level in the near future. Such advances are likely to be of major benefit in comprehending the roles the malfunctioning NPC plays in cancer, ageing, viral diseases, and neurodegeneration.© 2023 The Author(s).