ArticleBiophysical journal2014
Karyopherin-centric control of nuclear pores based on molecular occupancy and kinetic analysis of multivalent binding with FG nucleoporins.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed.
- Expandable DNA-origami rings as a nanomechanical platform for studying disordered nucleoporins.bioRxiv : the preprint server for biology · 2026Article
- Hydrophobic interactions of FG-nucleoporins are required for dilating nuclear membrane pores into selective transport channels after mitosis.Nature structural & molecular biology · 2026Article
- Unstructured but constructive FG repeats shape the nuclear pore complex architecture.Nature structural & molecular biology · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Kap-centric Nsp1-mediated nuclear transport at full amino acid resolution.Nature communications · 2025Article
- Elucidating the nanoscopic organization and dynamics of the nuclear pore complex.Nucleus (Austin, Tex.) · 2025Article
- Karyopherins remodel the dynamic organization of the nuclear pore complex transport barrier.Nature cell biology · 2025Article
- Article
- Selective phase separation of transcription factors is driven by orthogonal molecular grammar.Nature communications · 2025Article
- Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.Nucleus (Austin, Tex.) · 2024Review
- Channel width modulates the permeability of DNA origami-based nuclear pore mimics.Science advances · 2024Article
- The Effect of Dipeptide Repeat Proteins on FUS/TDP43-RNA Condensation in C9orf72 ALS/FTD.The journal of physical chemistry. B · 2024Article
- Channel width modulates the permeability of DNA origami based nuclear pore mimics.bioRxiv : the preprint server for biology · 2024Article
- Diameter dependence of transport through nuclear pore complex mimics studied using optical nanopores.eLife · 2024Article
- Mechanism of exportin retention in the cell nucleus.The Journal of cell biology · 2024Article
- A survey of the specificity and mechanism of 1,6 hexanediol-induced disruption of nuclear transport.Nucleus (Austin, Tex.) · 2023Article
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- Implications of a multiscale structure of the yeast nuclear pore complex.Molecular cell · 2023Article
- Article
- Improving the hole picture: towards a consensus on the mechanism of nuclear transport.Biochemical Society transactions · 2023Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered Phe-Gly nucleoporins (FG Nups) within nuclear pore complexes exert multivalent interactions with transport receptors (Karyopherins (Kaps)) that orchestrate nucleocytoplasmic transport. Current FG-centric views reason that selective Kap translocation is promoted by alterations in the barrier-like FG Nup conformations. However, the strong binding of Kaps with the FG Nups due to avidity contradicts rapid Kap translocation in vivo. Here, using surface plasmon resonance, we innovate a means to correlate in situ mechanistic (molecular occupancy and conformational changes) with equilibrium (binding affinity) and kinetic (multivalent binding kinetics) aspects of Karyopherinβ1 (Kapβ1) binding to four different FG Nups. A general feature of the FxFG domains of Nup214, Nup62, and Nup153 is their capacity to extend and accommodate large numbers of Kapβ1 molecules at physiological Kapβ1 concentrations. A notable exception is the GLFG domain of Nup98, which forms a partially penetrable cohesive layer. Interestingly, we find that a slowly exchanging Kapβ1 phase forms an integral constituent within the FG Nups that coexists with a fast phase, which dominates transport kinetics due to limited binding with the pre-occupied FG Nups at physiological Kapβ1 concentrations. Altogether, our data reveal an emergent Kap-centric barrier mechanism that may underlie mechanistic and kinetic control in the nuclear pore complex.
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