ArticleProceedings of the National Academy of Sciences of the United States of America2023
Self-regulation of the nuclear pore complex enables clogging-free crowded transport.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- The nuclear pore complex as a spatial organizing hub for high-risk DNA lesions.Nucleus (Austin, Tex.) · 2026Review
- Kap-centric Nsp1-mediated nuclear transport at full amino acid resolution.Nature communications · 2025Article
- Karyopherins remodel the dynamic organization of the nuclear pore complex transport barrier.Nature cell biology · 2025Article
- 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
- Article
- Charge of karyopherins and nuclear FG-Nups are key ingredients of nucleocytoplasmic transport.Biophysical journal · 2025Article
- Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.Nucleus (Austin, Tex.) · 2024Review
- 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
- Article
- Kinetic cooperativity resolves bidirectional clogging within the nuclear pore complex.Biophysical journal · 2024Article
- The Molecular Architecture of the Nuclear Basket.bioRxiv : the preprint server for 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
- Physical model of the nuclear membrane permeability mechanism.Biophysical reviews · 2023Review
- Improving the hole picture: towards a consensus on the mechanism of nuclear transport.Biochemical Society transactions · 2023Article
- Dynamic molecular mechanism of the nuclear pore complex permeability barrier.bioRxiv : the preprint server for biology · 2023Article
- Article
- Effects of Sequence Composition, Patterning and Hydrodynamics on the Conformation and Dynamics of Intrinsically Disordered Proteins.International journal of molecular sciences · 2023Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear pore complexes (NPCs) are the main conduits for macromolecular transport into and out of the nucleus of eukaryotic cells. The central component of the NPC transport mechanism is an assembly of intrinsically disordered proteins (IDPs) that fills the NPC channel. The channel interior is further crowded by large numbers of simultaneously translocating cargo-carrying and free transport proteins. How the NPC can efficiently, rapidly, and selectively transport varied cargoes in such crowded conditions remains ill understood. Past experimental results suggest that the NPC is surprisingly resistant to clogging and that transport may even become faster and more efficient as the concentration of transport protein increases. To understand the mechanisms behind these puzzling observations, we construct a computational model of the NPC comprising only a minimal set of commonly accepted consensus features. This model qualitatively reproduces the previous experimental results and identifies self-regulating mechanisms that relieve crowding. We show that some of the crowding-alleviating mechanisms-such as preventing saturation of the bulk flux-are "robust" and rely on very general properties of crowded dynamics in confined channels, pertaining to a broad class of selective transport nanopores. By contrast, the counterintuitive ability of the NPC to leverage crowding to achieve more efficient single-molecule translocation is "fine-tuned" and relies on the particular spatial architecture of the IDP assembly in the NPC channel.
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