ArticleeLife2019
Importin-9 wraps around the H2A-H2B core to act as nuclear importer and histone chaperone.
Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Palmitoyl Acyltransferase Zdhhc17 Promotes Functional Recovery After Spinal Cord Injury by Targeting the Nuclear Transport Factors Kpna2 and Ipo9.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Nucleosome Assembly Protein 1 in Dinoflagellate Cells Without Architectural Nucleosomes.International journal of molecular sciences · 2026Article
- Cleavage of histone H2A during embryonic stem cell differentiation destabilizes nucleosomes to counteract gene activation.The Journal of biological chemistry · 2026Article
- Bound for the nucleus: defining the molecular principles of cargo selection by importin 9.bioRxiv : the preprint server for biology · 2026Article
- Importin-9 recognizes the winged-helix fold of ETS transcription factors to mediate nuclear import.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A multivalent adaptor mechanism drives the nuclear import of proteasomes.Nature communications · 2026Article
- Histone Nuclear Import and Beyond: Multifunctional Roles of Importins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Importins recognize the winged-helix fold of ETS transcription factors to mediate nuclear import.bioRxiv : the preprint server for biology · 2026Article
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- A revised model of nuclear actin import: Importin 9 competes with cofilin, profilin, and RanGTP for actin binding.bioRxiv : the preprint server for biology · 2025Article
- Importin-9 and a TPR domain protein MpH drive periodic patterning of ciliary arrays in Tetrahymena.The Journal of cell biology · 2025Article
- Nap1 and Kap114 co-chaperone H2A-H2B and facilitate targeted histone release in the nucleus.The Journal of cell biology · 2025Article
- Stepwise order in protein complex assembly: approaches and emerging themes.Open biology · 2025Review
- Proteomic analysis of crocodile white blood cells reveals insights into the mechanism of the innate immune system.Heliyon · 2024Article
- Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD.Molecular neurodegeneration · 2024Review
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- Structural convergence endows nuclear transport receptor Kap114p with a transcriptional repressor function toward TATA-binding protein.Nature communications · 2023Article
- Molecular basis of RanGTP-activated release of Histones H2A-H2B from Importin-9.Structure (London, England : 1993) · 2023Article
- Mechanism of RanGTP priming H2A-H2B release from Kap114 in an atypical RanGTP•Kap114•H2A-H2B complex.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Co-translational binding of importins to nascent proteins.Nature communications · 2023Article
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Authors and funding
10 authors.
Funding
Abstract
We report the crystal structure of nuclear import receptor Importin-9 bound to its cargo, the histones H2A-H2B. Importin-9 wraps around the core, globular region of H2A-H2B to form an extensive interface. The nature of this interface coupled with quantitative analysis of deletion mutants of H2A-H2B suggests that the NLS-like sequences in the H2A-H2B tails play a minor role in import. Importin-9•H2A-H2B is reminiscent of interactions between histones and histone chaperones in that it precludes H2A-H2B interactions with DNA and H3-H4 as seen in the nucleosome. Like many histone chaperones, which prevent inappropriate non-nucleosomal interactions, Importin-9 also sequesters H2A-H2B from DNA. Importin-9 appears to act as a storage chaperone for H2A-H2B while escorting it to the nucleus. Surprisingly, RanGTP does not dissociate Importin-9•H2A-H2B but assembles into a RanGTP•Importin-9•H2A-H2B complex. The presence of Ran in the complex, however, modulates Imp9-H2A-H2B interactions to facilitate its dissociation by DNA and assembly into a nucleosome.
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