ArticleRNA (New York, N.Y.)2007
Specific trans-acting proteins interact with auxiliary RNA polyadenylation elements in the COX-2 3'-UTR.
Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 89 citations in OpenAlex.
- A conserved 3'UTR short motif regulates gene expression in vertebrates.Nucleic acids research · 2026Article
- Alternative cleavage and polyadenylation: key regulatory mechanisms in health and disease.RNA biology · 2025Review
- RNA binding proteins as mediators of pathological cardiac remodeling.Frontiers in cell and developmental biology · 2024Review
- PACER lncRNA regulates COX-2 expression in lung cancer cells.Oncotarget · 2022Article
- SFPQ rescues F508del-CFTR expression and function in cystic fibrosis bronchial epithelial cells.Scientific reports · 2021Article
- Protein-DNA/RNA Interactions: An Overview of Investigation Methods in the -Omics Era.Journal of proteome research · 2021Review
- A conserved role for the ALS-linked splicing factor SFPQ in repression of pathogenic cryptic last exons.Nature communications · 2021Article
- PRMT5 methylome profiling uncovers a direct link to splicing regulation in acute myeloid leukemia.Nature structural & molecular biology · 2019Article
- Cell Cycle Kinase Polo Is Controlled by a Widespread 3' Untranslated Region Regulatory Sequence in Drosophila melanogaster.Molecular and cellular biology · 2019Article
- Regulation of Eicosanoid Pathways by MicroRNAs.Frontiers in pharmacology · 2019Review
- Regulation of Kv11.1 potassium channel C-terminal isoform expression by the RNA-binding proteins HuR and HuD.The Journal of biological chemistry · 2018Article
- miR-146a suppresses 5-lipoxygenase activating protein (FLAP) expression and Leukotriene B4 production in lung cancer cells.Oncotarget · 2018Article
- RNA Degradation in Neurodegenerative Disease.Advances in neurobiology · 2018Review
- Review
- Article
- CD5 expression is regulated during human T-cell activation by alternative polyadenylation, PTBP1, and miR-204.European journal of immunology · 2016Article
- A crystallographic study of human NONO (p54(nrb)): overcoming pathological problems with purification, data collection and noncrystallographic symmetry.Acta crystallographica. Section D, Structural biology · 2016Article
- Processing and transcriptome expansion at the mRNA 3' end in health and disease: finding the right end.Pflugers Archiv : European journal of physiology · 2016Review
- The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular scaffold.Nucleic acids research · 2016Article
- The RNA-binding protein SFPQ orchestrates an RNA regulon to promote axon viability.Nature neuroscience · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two cyclooxygenase (COX) enzymes, COX-1 and COX-2, are present in human cells. While COX-1 is constitutively expressed, COX-2 is inducible and up-regulated in response to many signals. Since increased transcriptional activity accounts for only part of COX-2 up-regulation, we chose to explore other RNA processing mechanisms in the regulation of this gene. Previously, we showed that COX-2 is regulated by alternative polyadenylation, and that the COX-2 proximal polyadenylation signal contains auxiliary upstream sequence elements (USEs) that are very important in efficient polyadenylation. To explore trans-acting protein factors interacting with these cis-acting RNA elements, we performed pull-down assays with HeLa nuclear extract and biotinylated RNA oligonucleotides representing COX-2 USEs. We identified PSF, p54(nrb), PTB, and U1A as proteins specifically bound to the COX-2 USEs. We further explored their participation in polyadenylation using MS2 phage coat protein-MS2 RNA binding site tethering assays, and found that tethering any of these four proteins to the COX-2 USE mutant RNA can compensate for these cis-acting elements. Finally, we suggest that these proteins (p54(nrb), PTB, PSF, and U1A) may interact as a complex since immunoprecipitations of the transfected MS2 fusion proteins coprecipitate the other proteins.
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Registered trials
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.