ArticleCell cycle (Georgetown, Tex.)2012
Alternatively spliced protein arginine methyltransferase 1 isoform PRMT1v2 promotes the survival and invasiveness of breast cancer cells.
Article in Cell cycle (Georgetown, Tex.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Alternative splicing rewires breast cancer and opens therapeutic avenues.Cell communication and signaling : CCS · 2026Review
- Targeting the PRMT1 axis in cancer: from epigenetic plasticity to contextual therapeutic interventions.Frontiers in oncology · 2026Review
- Article
- Discovery of novel PRMT1 inhibitors: a combined approach using AI classification model and traditional virtual screening.Frontiers in chemistry · 2025Article
- PRMT1 in human neoplasm: cancer biology and potential therapeutic target.Cell communication and signaling : CCS · 2024Review
- A super-enhancer-regulated RNA-binding protein cascade drives pancreatic cancer.Nature communications · 2023Article
- Application of Quantitative Structure-Activity Relationships in the Prediction of New Compounds with Anti-Leukemic Activity.International journal of molecular sciences · 2023Article
- Protein arginine methylation in transcription and epigenetic regulation.Frontiers in epigenetics and epigenomics · 2023Review
- Arginine methylation in the epithelial-to-mesenchymal transition.The FEBS journal · 2022Review
- A peptoid-based inhibitor of protein arginine methyltransferase 1 (PRMT1) induces apoptosis and autophagy in cancer cells.The Journal of biological chemistry · 2022Article
- How Protein Methylation Regulates Steroid Receptor Function.Endocrine reviews · 2022Review
- PRMT1 Regulates EGFR and Wnt Signaling Pathways and Is a Promising Target for Combinatorial Treatment of Breast Cancer.Cancers · 2022Article
- Methylation of dual-specificity phosphatase 4 controls cell differentiation.Cell reports · 2021Article
- Naegleria fowleri: Protein structures to facilitate drug discovery for the deadly, pathogenic free-living amoeba.PloS one · 2021Article
- Hepatocellular Protein Arginine Methyltransferase 1 Suppresses Alcohol-Induced Hepatocellular Carcinoma Formation by Inhibition of Inducible Nitric Oxide Synthase.Hepatology communications · 2020Article
- PRMT1-mediated methylation of the microprocessor-associated proteins regulates microRNA biogenesis.Nucleic acids research · 2020Article
- The regulation, functions and clinical relevance of arginine methylation.Nature reviews. Molecular cell biology · 2019Review
- The Development of Tetrazole Derivatives as Protein Arginine Methyltransferase I (PRMT I) Inhibitors.International journal of molecular sciences · 2019Article
- Hepatocyte PRMT1 protects from alcohol induced liver injury by modulating oxidative stress responses.Scientific reports · 2019Article
- Mouse Models of Overexpression Reveal Distinct Oncogenic Roles for Different Type I Protein Arginine Methyltransferases.Cancer research · 2019Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Protein arginine methylation is catalyzed by protein arginine methyltransferases (PRMTs) and plays an important role in many cellular processes. Aberrant PRMT expression has been observed in several common cancer types; however, their precise contribution to the cell transformation process is not well understood. We previously reported that the PRMT1 gene generates several alternatively spliced isoforms, and our initial biochemical characterization of these isoforms revealed that they exhibit distinct substrate specificity and subcellular localization. We focus here on the PRMT1v2 isoform, which is the only predominantly cytoplasmic isoform, and we have found that its relative expression is increased in breast cancer cell lines and tumors. Specific depletion of PRMT1v2 using RNA interference caused a significant decrease in cancer cell survival due to an induction of apoptosis. Furthermore, depletion of PRMT1v2 in an aggressive cancer cell line significantly decreased cell invasion. We also demonstrate that PRMT1v2 overexpression in a non-aggressive cancer cell line was sufficient to render them more invasive. Importantly, this novel activity is specific to PRMT1v2, as overexpression of other isoforms did not enhance invasion. Moreover, this activity requires both proper subcellular localization and methylase activity. Lastly, PRMT1v2 overexpression altered cell morphology and reduced cell-cell adhesion, a phenomenon that we convincingly linked with reduced β-catenin protein expression. Overall, we demonstrate a specific role for PRMT1v2 in breast cancer cell survival and invasion, underscoring the importance of identifying and characterizing the distinct functional differences between PRMT1 isoforms.
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