ArticleMolecular & cellular proteomics : MCP2012
Nucleocytoplasmic transport: a role for nonspecific competition in karyopherin-nucleoporin interactions.
Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 66 citations in OpenAlex.
- HIV-1 capsid interactions with Nuclear Pore Complex components support nuclear entry via affinity gradient.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mechanoresponsive modulation of nuclear pore complex structure and function bybioRxiv : the preprint server for biology · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Translocation of HIV capsid core through the Nuclear Pore Complex by affinity gradient.bioRxiv : the preprint server for biology · 2025Article
- Regulating transport efficiency through the nuclear pore complex: The role of binding affinity with FG-Nups.Molecular biology of the cell · 2024Article
- Protein folding and quality control during nuclear transport.Current opinion in cell biology · 2024Review
- Improving the hole picture: towards a consensus on the mechanism of nuclear transport.Biochemical Society transactions · 2023Article
- Organelle-targeted therapies: a comprehensive review on system design for enabling precision oncology.Signal transduction and targeted therapy · 2022Review
- Crowding-induced phase separation of nuclear transport receptors in FG nucleoporin assemblies.eLife · 2022Article
- Synergies of Single Molecule Fluorescence and NMR for the Study of Intrinsically Disordered Proteins.Biomolecules · 2021Review
- The Great Escape: mRNA Export through the Nuclear Pore Complex.International journal of molecular sciences · 2021Review
- Characterizing Binding Interactions That Are Essential for Selective Transport through the Nuclear Pore Complex.International journal of molecular sciences · 2021Article
- DNA-Origami NanoTrap for Studying the Selective Barriers Formed by Phenylalanine-Glycine-Rich Nucleoporins.Journal of the American Chemical Society · 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
- New Family Members of FG Repeat Proteins and Their Unexplored Roles During Phase Separation.Frontiers in cell and developmental biology · 2021Review
- Poor old pores-The challenge of making and maintaining nuclear pore complexes in aging.The FEBS journal · 2020Review
- Design principles of selective transport through biopolymer barriers.Physical review. E · 2019Article
- Interactions of nuclear transport factors and surface-conjugated FG nucleoporins: Insights and limitations.PloS one · 2019Article
- In-Cell NMR within Budding Yeast Reveals Cytoplasmic Masking of Hydrophobic Residues of FG Repeats.Biophysical journal · 2018Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Nucleocytoplasmic transport occurs through the nuclear pore complex (NPC), which in yeast is a ~50 MDa complex consisting of ~30 different proteins. Small molecules can freely exchange through the NPC, but macromolecules larger than ~40 kDa must be aided across by transport factors, most of which belong to a related family of proteins termed karyopherins (Kaps). These transport factors bind to the disordered phenylalanine-glycine (FG) repeat domains in a family of NPC proteins termed FG nups, and this specific binding allows the transport factors to cross the NPC. However, we still know little in terms of the molecular and kinetic details regarding how this binding translates to selective passage of transport factors across the NPC. Here we show that the specific interactions between Kaps and FG nups are strongly modulated by the presence of a cellular milieu whose proteins appear to act as very weak competitors that nevertheless collectively can reduce Kap/FG nup affinities by several orders of magnitude. Without such modulation, the avidities between Kaps and FG nups measured in vitro are too tight to be compatible with the rapid transport kinetics observed in vivo. We modeled the multivalent interactions between the disordered repeat binding sites in the FG nups and multiple cognate binding sites on Kap, showing that they should indeed be sensitive to even weakly binding competitors; the introduction of such competition reduces the availability of these binding sites, dramatically lowering the avidity of their specific interactions and allowing rapid nuclear transport.
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Registered trials
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.