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Locking down the core of the pore

A highly stable heterotrimeric protein complex lines the central channel of the nuclear pore [Also see Research Article by Stuwe et al. and Report by Chug et al.] Nuclear pore complexes (NPCs), first observed by electron microscopy 65 years ago, mediate selective transport of macromolecules between the nucleus and cytoplasm of eukaryotic cells. Although the exact size and protein composition of NPCs can vary between species, these massive and complex machines are highly conserved in their overall organization, which consists of multiple copies of ∼30 nuclear pore proteins, or nucleoporins (Nups), in a symmetrical eightfold radial arrangement. Deciphering the structure of this immense complex has required ongoing multifaceted approaches (1). On page 106 and 56 in this issue, Chug et al. (2) and Stuwe et al. (3), respectively, have employed parallel approaches in very distant species and arrived at remarkably similar and informative structures of an essential subcomplex of the NPC.