ArticleNature communications2016
Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A.
Article in Nature communications, 2016. 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, 60 citations in OpenAlex.
- Regulation of Inducible Nitric Oxide Synthase (NOS2) Expression in Healthy and Inflamed Bowel: A Narrative Review.International journal of molecular sciences · 2026Review
- eIF5A coordinates the transcription and translation of its target genes.Cellular and molecular life sciences : CMLS · 2026Article
- A Deep-Learning Atlas of XPO1-Mediated Nuclear Export at Proteome Scale.bioRxiv : the preprint server for biology · 2026Article
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Analysis of exportins expression unveils their prognostic significance in colon adenocarcinoma: insights from public databases.Discover oncology · 2025Article
- DDX RNA helicases: key players in cellular homeostasis and innate antiviral immunity.Journal of virology · 2024Review
- TMCO1 is upregulated in breast cancer and regulates the response to pro-apoptotic agents in breast cancer cells.Cell death discovery · 2024Article
- Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD.Molecular neurodegeneration · 2024Review
- SUMOylation modulates eIF5A activities in both yeast and pancreatic ductal adenocarcinoma cells.Cellular & molecular biology letters · 2024Article
- Two Faces of Glutaminase GLS2 in Carcinogenesis.Cancers · 2023Review
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- Investigation of enzalutamide, docetaxel, and cabazitaxel resistance in the castration resistant prostate cancer cell line C4 using genome-wide CRISPR/Cas9 screening.Scientific reports · 2023Article
- A genome-wide CRISPR functional survey of the human phagocytosis molecular machinery.Life science alliance · 2023Article
- Cryo-EM structure of human eIF5A-DHS complex reveals the molecular basis of hypusination-associated neurodegenerative disorders.Nature communications · 2023Article
- Comparison of Human Eukaryotic Translation Initiation Factors 5A1 and 5AL1: Identification of Amino Acid Residues Important for EIF5A1 Lysine 50 Hypusination and Its Protein Stability.International journal of molecular sciences · 2023Article
- Identification of the Karyopherin Superfamily in Maize and Its Functional Cues in Plant Development.International journal of molecular sciences · 2022Review
- Exportin 4 depletion leads to nuclear accumulation of a subset of circular RNAs.Nature communications · 2022Article
- Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022Review
- Role of eIF5A in Mitochondrial Function.International journal of molecular sciences · 2022Review
- eIF5A is activated by virus infection or dsRNA and facilitates virus replication through modulation of interferon production.Frontiers in cellular and infection microbiology · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Xpo4 is a bidirectional nuclear transport receptor that mediates nuclear export of eIF5A and Smad3 as well as import of Sox2 and SRY. How Xpo4 recognizes such a variety of cargoes is as yet unknown. Here we present the crystal structure of the RanGTP·Xpo4·eIF5A export complex at 3.2 Å resolution. Xpo4 has a similar structure as CRM1, but the NES-binding site is occluded, and a new interaction site evolved that recognizes both globular domains of eIF5A. eIF5A contains hypusine, a unique amino acid with two positive charges, which is essential for cell viability and eIF5A function in translation. The hypusine docks into a deep, acidic pocket of Xpo4 and is thus a critical element of eIF5A's complex export signature. This further suggests that Xpo4 recognizes other cargoes differently, and illustrates how Xpo4 suppresses - in a chaperone-like manner - undesired interactions of eIF5A inside nuclei.
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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.