FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
- PMID: 17082456
- DOI: 10.1126/science.1132516
FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
Abstract
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.
Comment in
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Cell biology. Nuclear pore complex models gel.Science. 2006 Nov 3;314(5800):766-7. doi: 10.1126/science.1135739. Science. 2006. PMID: 17082440 No abstract available.
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Materials science. Polymers in the pore.Science. 2006 Nov 3;314(5800):766-7. doi: 10.1126/science.1135924. Science. 2006. PMID: 17082441 No abstract available.
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