Structural biology of nucleocytoplasmic transport

Atlanta Cook, Fulvia Bono, Martin Jinek, Elena Conti

Research output: Contribution to journalArticlepeer-review


In eukaryotic cells, segregation of DNA replication and RNA biogenesis in the nucleus and protein synthesis in the cytoplasm poses the requirement of transporting thousands of macromolecules between the two cellular compartments. Transport between nucleus and cytoplasm is mediated by soluble receptors that recognize specific cargoes and carry them through the nuclear pore complex (NPC), the sole gateway between the two compartments at interphase. Nucleocytoplasmic transport is specific not only in terms of cargo recognition, but also in terms of directionality, with nuclear proteins imported into the nucleus and RNAs exported from it. How is directionality achieved? How can the receptors be both specific and versatile in recognizing a multitude of cargoes? And how can their interaction with NPCs allow fast translocation? We describe the molecular mechanisms underlying nucleocytoplasmic transport as they have been revealed by structural studies of the receptors and regulators in different steps of transport cycles.
Original languageEnglish
Pages (from-to)647-71
Number of pages25
JournalAnnual review of biochemistry
Publication statusPublished - 2007


  • Active Transport, Cell Nucleus
  • Animals
  • Guanosine Triphosphate
  • Humans
  • Karyopherins
  • Models, Molecular
  • Nuclear Localization Signals
  • Nuclear Pore
  • Nuclear Pore Complex Proteins
  • Nuclear Proteins
  • Nucleocytoplasmic Transport Proteins
  • Protein Binding
  • Protein Conformation
  • RNA Cap-Binding Proteins
  • RNA, Messenger
  • Receptors, Cytoplasmic and Nuclear
  • Saccharomyces cerevisiae Proteins
  • beta Karyopherins
  • ran GTP-Binding Protein


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