Architecture of the fungal nuclear pore inner ring complex

Science. 2015 Oct 2;350(6256):56-64. doi: 10.1126/science.aac9176. Epub 2015 Aug 27.


The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional nucleocytoplasmic transport. We present the reconstitution and interdisciplinary analyses of the ~425-kilodalton inner ring complex (IRC), which forms the central transport channel and diffusion barrier of the NPC, revealing its interaction network and equimolar stoichiometry. The Nsp1•Nup49•Nup57 channel nucleoporin heterotrimer (CNT) attaches to the IRC solely through the adaptor nucleoporin Nic96. The CNT•Nic96 structure reveals that Nic96 functions as an assembly sensor that recognizes the three-dimensional architecture of the CNT, thereby mediating the incorporation of a defined CNT state into the NPC. We propose that the IRC adopts a relatively rigid scaffold that recruits the CNT to primarily form the diffusion barrier of the NPC, rather than enabling channel dilation.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Chaetomium / metabolism
  • Chaetomium / ultrastructure*
  • Fungal Proteins / chemistry
  • Fungal Proteins / ultrastructure*
  • Molecular Sequence Data
  • Nuclear Pore / metabolism
  • Nuclear Pore / ultrastructure*
  • Nuclear Pore Complex Proteins / chemistry
  • Nuclear Pore Complex Proteins / ultrastructure*
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / ultrastructure*
  • Protein Binding
  • Protein Multimerization
  • Protein Structure, Secondary
  • Protein Structure, Tertiary


  • Fungal Proteins
  • Nuclear Pore Complex Proteins
  • Nuclear Proteins

Associated data

  • PDB/4JNU
  • PDB/4JNV
  • PDB/4JO7
  • PDB/4JO9
  • PDB/4JQ5
  • PDB/5CWS
  • PDB/5CWT
  • PDB/5CWU
  • PDB/5CWV
  • PDB/5CWW