ArticleProceedings of the National Academy of Sciences of the United States of America2025
Integrative mapping reveals molecular features underlying the mechanism of nucleocytoplasmic transport.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Mechanotransduction by nuclear envelope tension.Nucleus (Austin, Tex.) · 2026Review
- Hydrophobic interactions of FG-nucleoporins are required for dilating nuclear membrane pores into selective transport channels after mitosis.Nature structural & molecular biology · 2026Article
- Karyopherins remodel the dynamic organization of the nuclear pore complex transport barrier.Nature cell biology · 2025Article
- Integrative mapping reveals molecular features underlying the mechanism of nucleocytoplasmic transport.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Hydrophobic interactions of FG-nucleoporins are required for dilating nuclear membrane pores into selective transport channels after mitosis.bioRxiv : the preprint server for biology · 2025Article
- Protein folding and quality control during nuclear transport.Current opinion in cell biology · 2024Review
- Integrative spatiotemporal modeling of biomolecular processes: application to the assembly of the Nuclear Pore Complex.bioRxiv : the preprint server for biology · 2024Article
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12 authors.
Funding
Abstract
Nuclear pore complexes (NPCs) enable rapid, selective, and robust nucleocytoplasmic transport. To explain how transport emerges from the system components and their interactions, we used experimental data and theoretical information to construct an integrative Brownian dynamics model of transport through an NPC, coupled to a kinetic model of transport in the cell. The model recapitulates key aspects of transport for a wide range of molecular cargoes, including preribosomes and viral capsids. Our model quantifies how flexible phenylalanine-glycine (FG) repeat proteins create an entropic barrier to passive diffusion and how this barrier is selectively lowered in facilitated diffusion by the many transient interactions of nuclear transport receptors with the FG repeats. Selective transport is enhanced by "fuzzy" multivalent interactions, redundant FG repeat mass, coupling to the energy-dependent RanGTP concentration gradient, and exponential dependence of transport kinetics on the transport barrier. Our model will facilitate rational modulation of the NPC and its artificial mimics.
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Registered trials
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