ArticleProceedings of the National Academy of Sciences of the United States of America2018
Structural-functional interactions of NS1-BP protein with the splicing and mRNA export machineries for viral and host gene expression.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Basigin (CD147) and calpain 4 (CapnS1) are partners in the generation of traction force but not in mechanosensing.The Journal of biological chemistry · 2026Article
- Tripartite motif-containing 34 (TRIM34) protein interacts with the nucleocytoplasmic transport machinery and negatively modulates antiviral responses.PLoS pathogens · 2026Article
- IVNS1ABP mutation drives cellular senescence in newly identified progeroid neuropathy.Nature communications · 2026Article
- Transcriptomic study of WSSV infection in Litopenaeus vannamei lymphoid organ via single nuclei RNA sequencing.PloS one · 2026Article
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Cellular hnRNP AB inhibits avian influenza virus RNA synthesis via blocking UAP56-mediated nuclear export of PB2 mRNA.Veterinary research · 2025Article
- SARS-CoV-2 Orf6 is positioned in the nuclear pore complex by Rae1 to inhibit nucleocytoplasmic transport.Molecular biology of the cell · 2024Article
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- Structural basis for high-order complex of SARNP and DDX39B to facilitate mRNP assembly.Cell reports · 2023Article
- Dancing with the Devil: A Review of the Importance of Host RNA-Binding Proteins to Alphaviral RNAs during Infection.Viruses · 2023Review
- SRSF5-Mediated Alternative Splicing of M Gene is Essential for Influenza A Virus Replication: A Host-Directed Target Against Influenza Virus.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Viral-host interactions during splicing and nuclear export of influenza virus mRNAs.Current opinion in virology · 2022Review
- Nuclear speckle integrity and function require TAO2 kinase.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A Review and Meta-Analysis of Influenza Interactome Studies.Frontiers in microbiology · 2022Review
- SYNCRIP facilitates porcine parvovirus viral DNA replication through the alternative splicing of NS1 mRNA to promote NS2 mRNA formation.Veterinary research · 2021Article
- Environmental Risk Assessment of Recombinant Viral Vector Vaccines against SARS-Cov-2.Vaccines · 2021Review
- Challenges and Limitations of Targeting the Keap1-Nrf2 Pathway for Neurotherapeutics: Bach1 De-Repression to the Rescue.Frontiers in aging neuroscience · 2021Review
- SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Chemical intervention of influenza virus mRNA nuclear export.PLoS pathogens · 2020Article
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Authors and funding
13 authors.
Funding
Abstract
The influenza virulence factor NS1 protein interacts with the cellular NS1-BP protein to promote splicing and nuclear export of the viral M mRNAs. The viral M1 mRNA encodes the M1 matrix protein and is alternatively spliced into the M2 mRNA, which is translated into the M2 ion channel. These proteins have key functions in viral trafficking and budding. To uncover the NS1-BP structural and functional activities in splicing and nuclear export, we performed proteomics analysis of nuclear NS1-BP binding partners and showed its interaction with constituents of the splicing and mRNA export machineries. NS1-BP BTB domains form dimers in the crystal. Full-length NS1-BP is a dimer in solution and forms at least a dimer in cells. Mutations suggest that dimerization is important for splicing. The central BACK domain of NS1-BP interacts directly with splicing factors such as hnRNP K and PTBP1 and with the viral NS1 protein. The BACK domain is also the site for interactions with mRNA export factor Aly/REF and is required for viral M mRNA nuclear export. The crystal structure of the C-terminal Kelch domain shows that it forms a β-propeller fold, which is required for the splicing function of NS1-BP. This domain interacts with the polymerase II C-terminal domain and SART1, which are involved in recruitment of splicing factors and spliceosome assembly, respectively. NS1-BP functions are not only critical for processing a subset of viral mRNAs but also impact levels and nuclear export of a subset of cellular mRNAs encoding factors involved in metastasis and immunity.
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