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FG-Rich Repeats of Nuclear Pore Proteins Form a Three-Dimensional Meshwork with Hydrogel-Like Properties

Open access
Frey, Steffen, Richter, Ralf P., Görlich, Dirk·2006·Science

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.

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Metadata

Authors
Frey, S., Richter, R. P., & Görlich, D.
Venue
Science
Published
2006-11-03
Volume
314
Issue
5800
Pages
815-817
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2076870182
Cited by
688
References
0
FWCI
10.56
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: FG-Rich Repeats of Nuclear Pore Proteins Form a Three-Dimensional Meshwork with Hydrogel-Like Properties. https://app.cochat.ai/papers/10.1126/science.1132516
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Frey, S., Richter, R. P., & Görlich, D. (2006). FG-Rich Repeats of Nuclear Pore Proteins Form a Three-Dimensional Meshwork with Hydrogel-Like Properties. Science. https://doi.org/10.1126/science.1132516

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.