ArticleNature cell biology2024
Docking a flexible basket onto the core of the nuclear pore complex.
Article in Nature cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- A tool to pulse-label yeast nuclear pore complexes in imaging and biochemical experiments.eLife · 2026Article
- Mlp1 and Mlp2 cooperate to build a stoichiometric nuclear pore basket in budding yeast.Journal of cell science · 2026Article
- Synaptonemal complex SUMOylation is maintained by Nup60-dependent docking of Ulp1 at the nuclear periphery.Cell reports · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Structural mechanism of DDX39B regulation by human TREX-2 and a related complex in mRNP remodeling.Nature communications · 2025Article
- Ulp1 association with nuclear pore complexes is required for the maintenance of global SUMOylation.Molecular biology of the cell · 2025Article
- Detailed characterisation of the trypanosome nuclear pore architecture reveals conserved asymmetrical functional hubs that drive mRNA export.PLoS biology · 2025Article
- From the Cytoplasm into the Nucleus-Hepatitis B Virus Travel and Genome Repair.Microorganisms · 2025Review
- Nuclear basket proteins regulate the distribution and mobility of nuclear pore complexes in budding yeast.Molecular biology of the cell · 2024Article
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Authors and funding
2 authors.
Funding
Abstract
The nuclear basket attaches to the nucleoplasmic side of the nuclear pore complex (NPC), coupling transcription to mRNA quality control and export. The basket expands the functional repertoire of a subset of NPCs in Saccharomyces cerevisiae by drawing a unique RNA/protein interactome. Yet, how the basket docks onto the NPC core remains unknown. By integrating AlphaFold-based interaction screens, electron microscopy and membrane-templated reconstitution, we uncovered a membrane-anchored tripartite junction between basket and NPC core. The basket subunit Nup60 harbours three adjacent short linear motifs, which connect Mlp1, a parallel homodimer consisting of coiled-coil segments interrupted by flexible hinges, and the Nup85 subunit of the Y-complex. We reconstituted the Y-complex•Nup60•Mlp1 assembly on a synthetic membrane and validated the protein interfaces in vivo. Here we explain how a short linear motif-based protein junction can substantially reshape NPC structure and function, advancing our understanding of compositional and conformational NPC heterogeneity.
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Registered trials
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