ArticleThe Journal of cell biology2020
The liquid state of FG-nucleoporins mimics permeability barrier properties of nuclear pore complexes.
Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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Who cites it
87 citing papers in PubMed, 152 citations in OpenAlex.
- Hydrophobic interactions of FG-nucleoporins are required for dilating nuclear membrane pores into selective transport channels after mitosis.Nature structural & molecular biology · 2026Article
- A practical guide to investigating biomolecular condensates: a comment from the plant community.Science China. Life sciences · 2026Review
- A Unifying Thermodynamic Model for Phase Separation and Aging of Biopolymers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Mechanoresponsive modulation of nuclear pore complex structure and function bybioRxiv : the preprint server for biology · 2026Article
- Sensing and Filtering Environmental Fluctuations: The Case of Biomolecular Condensates in Plants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Super-Resolution Imaging of Nuclear Pore Responses to Mechanical Stress and Energy Depletion.Viruses · 2026Article
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- Biomolecular condensates as cellular memory modules: Thermodynamic principles and plant stress adaptation.Biophysical journal · 2026Review
- Nuclear-Cytoplasmic Axis in Cancer: From Protein Mislocalization to Anticancer Drug Resistance.Oncology research · 2026Review
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Effects of Nanopore Confinement on the Conformational, Dynamical, and Self-Assembly Properties of an FG-Repeat Peptide.The journal of physical chemistry. B · 2025Article
- Kap-centric Nsp1-mediated nuclear transport at full amino acid resolution.Nature communications · 2025Article
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Karyopherins remodel the dynamic organization of the nuclear pore complex transport barrier.Nature cell biology · 2025Article
- Effects of Nanopore Confinement on the Conformational, Dynamical, and Self-Assembly Properties of an FG-Repeat Peptide.bioRxiv : the preprint server for biology · 2025Article
- Differential conformational expansion of NUP98-HOXA9 oncoprotein from nanosized assemblies to macrophases.Nature communications · 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
- Sense, plug, and seal: proteins as both rapid responders and constitutive barriers supporting organelle compartmentalization.Molecular biology of the cell · 2025Review
- Induction and Manipulation of Biomolecular Condensates Through Spatially Heterogeneous Solution Conditions.Chembiochem : a European journal of chemical biology · 2025Article
- Role of pore dilation in molecular transport through the nuclear pore complex: Insights from polymer scaling theory.PLoS computational biology · 2025Article
27 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear pore complexes (NPCs) regulate all cargo traffic across the nuclear envelope. The transport conduit of NPCs is highly enriched in disordered phenylalanine/glycine-rich nucleoporins (FG-Nups), which form a permeability barrier of still elusive and highly debated molecular structure. Here we present a microfluidic device that triggered liquid-to-liquid phase separation of FG-Nups, which yielded droplets that showed typical properties of a liquid state. On the microfluidic chip, droplets were perfused with different transport-competent or -incompetent cargo complexes, and then the permeability barrier properties of the droplets were optically interrogated. We show that the liquid state mimics permeability barrier properties of the physiological nuclear transport pathway in intact NPCs in cells: that is, inert cargoes ranging from small proteins to large capsids were excluded from liquid FG-Nup droplets, but functional import complexes underwent facilitated import into droplets. Collectively, these data provide an experimental model of how NPCs can facilitate fast passage of cargoes across an order of magnitude in cargo size.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.