ArticleBiochimica et biophysica acta2014
A truncated hnRNP A1 isoform, lacking the RGG-box RNA binding domain, can efficiently regulate HIV-1 splicing and replication.
Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Backsplicing of the HIV-1 transcript generates multiple circRNAs to promote viral replication.Npj viruses · 2025Article
- Higher isoform of hnRNPA1 confer Temozolomide resistance in U87MG & LN229 glioma cells.Journal of neuro-oncology · 2025Article
- Article
- Let It Go: HIV-1Journal of virology · 2021Review
- Post-translational modifications of hnRNP A1 differentially modulate retroviral IRES-mediated translation initiation.Nucleic acids research · 2020Article
- Stress proteins: the biological functions in virus infection, present and challenges for target-based antiviral drug development.Signal transduction and targeted therapy · 2020Review
- The multifarious roles of heterogeneous ribonucleoprotein A1 in viral infections.Reviews in medical virology · 2020Review
- Scaffold attachment factor B suppresses HIV-1 infection of CD4The Journal of biological chemistry · 2018Article
- Contribution of the Degeneration of the Neuro-Axonal Unit to the Pathogenesis of Multiple Sclerosis.Brain sciences · 2017Review
- RNA-binding proteins with prion-like domains in health and disease.The Biochemical journal · 2017Review
- Can the HIV-1 splicing machinery be targeted for drug discovery?HIV/AIDS (Auckland, N.Z.) · 2017Review
- HIV-1 transcription is regulated by splicing factor SRSF1.Nucleic acids research · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is one of the most abundant RNA binding proteins. hnRNP A1 is localized prevalently in the nucleus but it can relocate to the cytoplasm in response to specific stimuli shuttling between nuclear and cytoplasmic compartments. The cellular localization of this protein is regulated by a short C-terminus motif (M9) and other less defined sequences. The RNA binding specificity of this protein is dependent on multiple RNA binding domains (RBDs), which regulate its role in RNA processing and expression. hnRNP A1 plays multiple roles in gene expression by regulating the biogenesis and translation of messengers RNAs, the processing of miRNAs, affecting transcription and controlling telomere maintenance. The multiple functions of this protein correlate with diverse roles in genetic disease, cancer and the replication of viral pathogens. Utilizing a tagged hnRNP A1 deletion library we have shown that the three hnRNP A1 RBDs contribute to the prevalent nuclear distribution of the protein. Our data also indicate that a truncated form of the protein, lacking one of the RBDs, the RGG-box, can regulate splicing of a splicing reporter minigene and down-regulate replication of the HIV-1 virus with efficiency comparable to the wild-type protein. This functional hnRNP A1 deletion mutant is similar to a predicted hnRNP A1 isoform, which had not been previously experimentally characterized.
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