ArticleNature communications2025
Kap-centric Nsp1-mediated nuclear transport at full amino acid resolution.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- FgNup2 regulates nuclear import of the histone H2B monoubiquitination enzyme by stabilizing the FgImpα-FgBre1 complex to mediate pathogenicity in Fusarium graminearum.PLoS pathogens · 2026Article
- Mechanoresponsive modulation of nuclear pore complex structure and function bybioRxiv : the preprint server for biology · 2026Article
- Toward an integrated view of nuclear pore transport.Trends in cell biology · 2026Review
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- Karyopherins remodel the dynamic organization of the nuclear pore complex transport barrier.Nature cell biology · 2025Article
- RNA-Protein Assemblies: A Review of Biophysical Principles and Coarse-Grained Modeling Approaches.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Recent studies of nuclear pore complexes (NPCs) have provided detailed descriptions of the core scaffold structures, yet fall short in resolving the dynamic FG meshwork with similar precision. Here, we present an amino acid resolution model that enables full-scale simulations of selective transport through the NPC. We map the spatial distributions and nanosecond dynamics of individual FG-Nups in the central transporter, revealing that the bimodal architecture of Nsp1 forms a dynamic central meshwork essential for regulating both passive and active transport. Incorporating nuclear transport receptors (NTRs), specifically Kap95, shows that NTRs strengthen the permeability barrier by increasing the energetic cost of inert cargo translocation. Kaps exhibit alternating phases of binding and motion, moving through transient voids generated by FG fluctuations. Overall, our simulations identify a dense GLFG-ring coated by low-mobility Kaps and a dynamic central FG meshwork that together create a reduced-dimensional transport surface of optimal binding avidity that drives Kap translocation.
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Registered trials
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