PerspectiveStructural Biology

Locking down the core of the pore

See allHide authors and affiliations

Science  02 Oct 2015:
Vol. 350, Issue 6256, pp. 33-34
DOI: 10.1126/science.aad3797

You are currently viewing the summary.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution


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.