ArticleNucleic acids research2015
The principal mRNA nuclear export factor NXF1:NXT1 forms a symmetric binding platform that facilitates export of retroviral CTE-RNA.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 59 citations in OpenAlex.
- Article
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- Division of labor in trypanosome RNA processing and export through expanded Mex67 paralogs.Nucleic acids research · 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
- From transcription to export: mRNA's winding path to the cytoplasm.Trends in biochemical sciences · 2025Review
- Immune Escape-Related Gene NXT1 as a Potential Prognostic and Therapeutic Target in Hepatocellular Carcinoma.The Turkish journal of gastroenterology : the official journal of Turkish Society of Gastroenterology · 2025Article
- Participation of host cell proteins in inclusion bodies of non-segmented RNA virus infected cells: a molecular insight.Virology journal · 2025Review
- O-GlcNAc modulation of nuclear pore complexes orchestrates mRNA export efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural mechanism of DDX39B regulation by human TREX-2 and a related complex in mRNP remodeling.Nature communications · 2025Article
- Cell-Specific Transposable Element and Gene Expression Analysis Across Systemic Lupus Erythematosus Phenotypes.ACR open rheumatology · 2024Article
- Identification of RNA structures and their roles in RNA functions.Nature reviews. Molecular cell biology · 2024Review
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- Review
- Unraveling docking and initiation of mRNA export through the nuclear pore complex.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022Article
- Understanding COVID-19 Pathogenesis: A Drug-Repurposing Effort to Disrupt Nsp-1 Binding to Export Machinery Receptor Complex.Pathogens (Basel, Switzerland) · 2021Article
- The Great Escape: mRNA Export through the Nuclear Pore Complex.International journal of molecular sciences · 2021Review
- Selective Modulation of a Pan-Essential Protein as a Therapeutic Strategy in Cancer.Cancer discovery · 2021Article
- Evolution and diversification of the nuclear pore complex.Biochemical Society transactions · 2021Review
- Sequence-dependent recruitment of SRSF1 and SRSF7 to intronless lncRNA NKILA promotes nuclear export via the TREX/TAP pathway.Nucleic acids research · 2021Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The NXF1:NXT1 complex (also known as TAP:p15) is a general mRNA nuclear export factor that is conserved from yeast to humans. NXF1 is a modular protein constructed from four domains (RRM, LRR, NTF2-like and UBA domains). It is currently unclear how NXF1:NXT1 binds transcripts and whether there is higher organization of the NXF1 domains. We report here the 3.4 Å resolution crystal structure of the first three domains of human NXF1 together with NXT1 that has two copies of the complex in the asymmetric unit arranged to form an intimate domain-swapped dimer. In this dimer, the linkers between the NXF1 LRR and NTF2-like domains interact with NXT1, generating a 2-fold symmetric platform in which the RNA-binding RRM, LRR and NTF2-like domains are arranged on one face. In addition to bulk transcripts, NXF1:NXT1 also facilitates the export of unspliced retroviral genomic RNA from simple type-D retroviruses such as SRV-1 that contain a constitutive transport element (CTE), a cis-acting 2-fold symmetric RNA stem-loop motif. Complementary structural, biochemical and cellular techniques indicated that the formation of a symmetric RNA binding platform generated by dimerization of NXF1:NXT1 facilitates the recognition of CTE-RNA and promotes its nuclear export.
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Registered trials
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