ArticleProceedings of the National Academy of Sciences of the United States of America2022
Structure of IMPORTIN-4 bound to the H3-H4-ASF1 histone-histone chaperone complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 23 citations in OpenAlex.
- CAF-1 in Replication and Repair: A Critical Genetic Mediator of Synthesis-Coupled Nucleosome Assembly.Biomolecules · 2026Review
- Newly synthesized histones: passive or active players in the regulation of epigenetic inheritance?Nucleic acids research · 2026Review
- 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
- Exploration of the proxiOME of large subunit ribosomal proteins reveals Acl1 and Bcl1 as cooperating dedicated chaperones of Rpl1.Nucleic acids research · 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
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Histone supply: a precious commodity for cell identity.The Biochemical journal · 2025Review
- CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply.Nature communications · 2025Article
- TMCO1 is upregulated in breast cancer and regulates the response to pro-apoptotic agents in breast cancer cells.Cell death discovery · 2024Article
- Article
- 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
- 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
- Structure of IMPORTIN-4 bound to the H3-H4-ASF1 histone-histone chaperone complex.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A specific role for importin-5 and NASP in the import and nuclear hand-off of monomeric H3.eLife · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
IMPORTIN-4, the primary nuclear import receptor of core histones H3 and H4, binds the H3-H4 dimer and histone chaperone ASF1 prior to nuclear import. However, how H3-H3-ASF1 is recognized for transport cannot be explained by available crystal structures of IMPORTIN-4-histone tail peptide complexes. Our 3.5-Å IMPORTIN-4-H3-H4-ASF1 cryoelectron microscopy structure reveals the full nuclear import complex and shows a binding mode different from suggested by previous structures. The N-terminal half of IMPORTIN-4 clamps the globular H3-H4 domain and H3 αN helix, while its C-terminal half binds the H3 N-terminal tail weakly; tail contribution to binding energy is negligible. ASF1 binds H3-H4 without contacting IMPORTIN-4. Together, ASF1 and IMPORTIN-4 shield nucleosomal H3-H4 surfaces to chaperone and import it into the nucleus where RanGTP binds IMPORTIN-4, causing large conformational changes to release H3-H4-ASF1. This work explains how full-length H3-H4 binds IMPORTIN-4 in the cytoplasm and how it is released in the nucleus.
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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.