FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties

Science. 2006 Nov 3;314(5800):815-7. doi: 10.1126/science.1132516.


Nuclear pore complexes permit rapid passage of cargoes bound to nuclear transport receptors, but otherwise suppress nucleocytoplasmic fluxes of inert macromolecules >/=30 kilodaltons. To explain this selectivity, a sieve structure of the permeability barrier has been proposed that is created through reversible cross-linking between Phe and Gly (FG)-rich nucleoporin repeats. According to this model, nuclear transport receptors overcome the size limit of the sieve and catalyze their own nuclear pore-passage by a competitive disruption of adjacent inter-repeat contacts, which transiently opens adjoining meshes. Here, we found that phenylalanine-mediated inter-repeat interactions indeed cross-link FG-repeat domains into elastic and reversible hydrogels. Furthermore, we obtained evidence that such hydrogel formation is required for viability in yeast.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Biopolymers
  • Calcium-Binding Proteins / chemistry*
  • Calcium-Binding Proteins / genetics
  • Calcium-Binding Proteins / metabolism*
  • Fluorescence Recovery After Photobleaching
  • HeLa Cells
  • Humans
  • Hydrogels
  • Hydrogen-Ion Concentration
  • Hydrophobic and Hydrophilic Interactions
  • Models, Biological
  • Molecular Sequence Data
  • Mutation
  • Nuclear Pore / chemistry
  • Nuclear Pore / metabolism*
  • Nuclear Pore Complex Proteins / chemistry*
  • Nuclear Pore Complex Proteins / metabolism*
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Nucleocytoplasmic Transport Proteins / metabolism*
  • Permeability
  • Phenylalanine / chemistry
  • Protein Structure, Tertiary
  • Repetitive Sequences, Amino Acid
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / physiology
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*


  • Biopolymers
  • Calcium-Binding Proteins
  • Hydrogels
  • NSP1 protein, S cerevisiae
  • Nuclear Pore Complex Proteins
  • Nuclear Proteins
  • Nucleocytoplasmic Transport Proteins
  • Saccharomyces cerevisiae Proteins
  • Phenylalanine