ArticleProceedings of the National Academy of Sciences of the United States of America2017
Epigenetic control via allosteric regulation of mammalian protein arginine methyltransferases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 59 citations in OpenAlex.
- PRMT7 restricts CD8+ T cells expansion via the NF-ΚB pathway.Nature communications · 2026Article
- Arginine Methylation in Alternative Splicing: Implications for Cancer Therapy.Journal of cellular physiology · 2026Review
- Dapagliflozin binds PRMT7 to inhibit p38 MAPK phosphorylation and macrophage foam cell formation in atherosclerosis.iScience · 2026Article
- Protein arginine methyltransferase 5 as a novel therapeutic target in solid tumors.Genes & diseases · 2026Review
- Protein arginine methyltransferase 7 regulates the cell cycle and promotes the progression of prostate cancer.Oncology letters · 2025Article
- PRMT7-Mediated PTEN Activation Enhances Bone Regeneration in Female Mice.International journal of molecular sciences · 2025Article
- The roles and mechanisms of SREBP1 in cancer development and drug response.Genes & diseases · 2024Review
- Critical Roles of Protein Arginine Methylation in the Central Nervous System.Molecular neurobiology · 2023Review
- Research progress on PRMTs involved in epigenetic modification and tumour signalling pathway regulation (Review).International journal of oncology · 2023Review
- Arginine Methylation of the PGC-1α C-Terminus Is Temperature-Dependent.Biochemistry · 2023Article
- The exquisite specificity of human protein arginine methyltransferase 7 (PRMT7) toward Arg-X-Arg sites.PloS one · 2023Article
- Protein arginine methylation in viral infection and antiviral immunity.International journal of biological sciences · 2023Review
- 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
- Protein Arginine Methyltransferases as Therapeutic Targets in Hematological Malignancies.Cancers · 2022Review
- PRMT7 ablation stimulates anti-tumor immunity and sensitizes melanoma to immune checkpoint blockade.Cell reports · 2022Article
- PRMT5: a putative oncogene and therapeutic target in prostate cancer.Cancer gene therapy · 2022Review
- The Influence of Arginine Methylation in Immunity and Inflammation.Journal of inflammation research · 2022Review
- Effects of substrate modifications on the arginine dimethylation activities of PRMT1 and PRMT5.Epigenetics · 2022Article
- Cellular pathways influenced by protein arginine methylation: Implications for cancer.Molecular cell · 2021Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Arginine methylation on histones is a central player in epigenetics and in gene activation and repression. Protein arginine methyltransferase (PRMT) activity has been implicated in stem cell pluripotency, cancer metastasis, and tumorigenesis. The expression of one of the nine mammalian PRMTs, PRMT5, affects the levels of symmetric dimethylarginine (SDMA) at Arg-3 on histone H4, leading to the repression of genes which are related to disease progression in lymphoma and leukemia. Another PRMT, PRMT7, also affects SDMA levels at the same site despite its unique monomethylating activity and the lack of any evidence for PRMT7-catalyzed histone H4 Arg-3 methylation. We present evidence that PRMT7-mediated monomethylation of histone H4 Arg-17 regulates PRMT5 activity at Arg-3 in the same protein. We analyzed the kinetics of PRMT5 over a wide range of substrate concentrations. Significantly, we discovered that PRMT5 displays positive cooperativity in vitro, suggesting that this enzyme may be allosterically regulated in vivo as well. Most interestingly, monomethylation at Arg-17 in histone H4 not only raised the general activity of PRMT5 with this substrate, but also ameliorated the low activity of PRMT5 at low substrate concentrations. These kinetic studies suggest a biochemical explanation for the interplay between PRMT5- and PRMT7-mediated methylation of the same substrate at different residues and also suggest a general model for regulation of PRMTs. Elucidating the exact relationship between these two enzymes when they methylate two distinct sites of the same substrate may aid in developing therapeutics aimed at reducing PRMT5/7 activity in cancer and other diseases.
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Registered trials
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