Lighting up the nuclear pore complex

Eur J Cell Biol. 2011 Sep;90(9):751-8. doi: 10.1016/j.ejcb.2011.04.004. Epub 2011 May 31.


It is generally accepted that transport through the nuclear pore complex (NPC) involves an abundance of phenylalanine-glycine rich protein domains (FG-domains) that serve as docking sites for soluble nuclear transport receptors (NTRs) and their cargo complexes. But the precise mechanism of translocation through the NPC allowing for high speed and selectivity is still vividly debated. To ultimately decipher the underlying gating mechanism it is indispensable to shed more light on the molecular arrangement of FG-domains and the distribution of NTR-binding sites within the central channel of the NPC. In this review we revisit current transport models, summarize recent results regarding translocation through the NPC obtained by super-resolution microscopy and finally discuss the status and potential of optical methods in the analysis of the NPC.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Nuclear Pore / chemistry*
  • Nuclear Pore / metabolism
  • Nuclear Pore Complex Proteins / chemistry*
  • Nuclear Pore Complex Proteins / metabolism


  • Nuclear Pore Complex Proteins