Structure and Function of the Nuclear Pore Complex Cytoplasmic mRNA Export Platform

Cell. 2016 Nov 17;167(5):1215-1228.e25. doi: 10.1016/j.cell.2016.10.028. Epub 2016 Nov 10.


The last steps in mRNA export and remodeling are performed by the Nup82 complex, a large conserved assembly at the cytoplasmic face of the nuclear pore complex (NPC). By integrating diverse structural data, we have determined the molecular architecture of the native Nup82 complex at subnanometer precision. The complex consists of two compositionally identical multiprotein subunits that adopt different configurations. The Nup82 complex fits into the NPC through the outer ring Nup84 complex. Our map shows that this entire 14-MDa Nup82-Nup84 complex assembly positions the cytoplasmic mRNA export factor docking sites and messenger ribonucleoprotein (mRNP) remodeling machinery right over the NPC's central channel rather than on distal cytoplasmic filaments, as previously supposed. We suggest that this configuration efficiently captures and remodels exporting mRNP particles immediately upon reaching the cytoplasmic side of the NPC.

Keywords: Nup4 complex; Nup82 complex; computational structural biology; cross-linking and mass spectrometry; electron microscopy; integrative structure determination; mRNA export; mRNP remodeling; nuclear pore complex; small-angle X-ray scattering.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus
  • Fungal Proteins
  • Nuclear Pore / chemistry*
  • Nuclear Pore Complex Proteins / chemistry*
  • Nuclear Pore Complex Proteins / ultrastructure
  • RNA, Messenger
  • Saccharomyces cerevisiae / cytology
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Saccharomyces cerevisiae Proteins / ultrastructure
  • Yeasts / metabolism*


  • Fungal Proteins
  • Nuclear Pore Complex Proteins
  • RNA, Messenger
  • Saccharomyces cerevisiae Proteins