Solving the nuclear pore puzzle

Abstract

Using a battery of tools, the architecture of the nuclear pore complex is revealed

Abstract

In eukaryotic cells, the genome is sequestered in the nucleus, shielded from the cytoplasm by the double-layered nuclear envelope (NE). Transport of macromolecules across the NE occurs through nuclear pore complexes (NPCs), which perforate the NE at ∼200 to 2000 positions ( 1 – 3 ). Ions and molecules up to ∼40 kDa diffuse through NPCs, whereas larger cargo selectively associate with soluble nuclear transport factors to be ferried through the central NPC channel ( 4 ). But it has been unclear how NPCs exactly control the transport of a vast array of different substrates, including soluble proteins, embedded membrane proteins, RNAs, and even some viral capsids. On pages 1174, 1175, 1176, 1177, and 1178 of this issue, Bley et al.( 5 ), Petrovic et al.( 6 ), Mosalaganti et al.( 7 ), Zhu et al.( 8 ), and Fontana et al.( 9 ), respectively, now provide molecular structures, in unprecedented detail, of how NPCs are built. These findings will enable approaches to further dissect the many NPC functions.