ArticleBiophysical journal2013
Model inspired by nuclear pore complex suggests possible roles for nuclear transport receptors in determining its structure.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed.
- 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
- Morphology of Polymer Brushes in the Presence of Attractive Nanoparticles: Effects of Temperature.International journal of molecular sciences · 2023Article
- Crowding-induced phase separation of nuclear transport receptors in FG nucleoporin assemblies.eLife · 2022Article
- Free energy calculations shed light on the nuclear pore complex's selective barrier nature.Biophysical journal · 2021Article
- Physics of the Nuclear Pore Complex: Theory, Modeling and Experiment.Physics reports · 2021Article
- Physical modeling of multivalent interactions in the nuclear pore complex.Biophysical journal · 2021Article
- Article
- The Role of Cohesiveness in the Permeability of the Spatial Assemblies of FG Nucleoporins.Biophysical journal · 2019Article
- Article
- Protein Transport by the Nuclear Pore Complex: Simple Biophysics of a Complex Biomachine.Biophysical journal · 2017Review
- Article
- Article
- Energetics of Transport through the Nuclear Pore Complex.PloS one · 2016Article
- Evolutionarily Conserved Sequence Features Regulate the Formation of the FG Network at the Center of the Nuclear Pore Complex.Scientific reports · 2015Article
- Nanoscale stiffness topography reveals structure and mechanics of the transport barrier in intact nuclear pore complexes.Nature nanotechnology · 2015Article
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3 authors.
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Abstract
Nuclear transport receptors (NTRs) mediate nucleocytoplasmic transport via their affinity for unstructured proteins (polymers) in the nuclear pore complex (NPC). Here, we have modeled the effect of NTRs on polymeric structure in the nanopore confinement of the NPC central conduit. The model explicitly takes into account inter- and intramolecular interactions, as well as the finite size of the NTRs (∼20% of the NPC channel diameter). It reproduces various proposed scenarios for the channel structure, ranging from a central polymer condensate (selective phase) to brushlike polymer arrangements localized at the channel wall (virtual gate, reduction of dimensionality), with the transport receptors lining the polymer surface. In addition, it predicts a new structure in which NTRs become an integral part of the transport barrier by forming a cross-linked network with the unstructured proteins stretching across the pore. The model provides specific and distinctive predictions for the equilibrium spatial distributions of NTRs for these different scenarios that can be experimentally verified by, e.g., superresolution fluorescence microscopy. Moreover, it suggests mechanisms by which globular macromolecules (colloidal particles) can cause polymer-coated nanopores to switch between open and closed configurations, a possible explanation of the biological function of the NPC, and suggests potential technological applications for filtration and single-molecule sensing.
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