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Nuclear pore complexes (NPCs) mediate the exchange of materials between thenucleoplasm and cytoplasm, playing a key role in the separation of nucleicacids and proteins into their required compartments. The static structure ofthe NPC is relatively well defined by recent cryo EM and other studies. Thefunctional roles of dynamic components in the pore of the NPC,phenylalanyl-glycyl (FG) repeat rich nucleoporins, is less clear because of ourlimited understanding of highly dynamic protein systems. These proteins form arestrained concentrate which interacts with and concentrates nuclear transportfactors (NTRs) to provide facilitated nucleocytoplasmic transport of cargoes.Very rapid exchange among FG repeats and NTRs supports extremely fastfacilitated transport, close to the rate of macromolecular diffusion incytoplasm, while complexes without specific interactions are entropicallyexcluded, though details on several aspects of the transport mechanism and FGrepeat behaviors remain to be resolved. However, as discussed here, newtechnical approaches combined with more advanced modeling methods will likelyprovide an improved dynamic description of NPC transport, potentially at theatomic level in the near future. Such advances are likely to be of majorbenefit in comprehending the roles the malfunctioning NPC plays in cancer,aging, viral diseases, and neurodegeneration.

Improving the Hole Picture: Towards a Consensus on the Mechanism of Nuclear Transport