{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nProtein arginine methyltransferase 1 (PRMT1) is the predominant enzyme catalyzing asymmetric dimethylation of arginine residues on both histone and non‐histone substrates. Through this activity, PRMT1 regulates chromatin structure, transcriptional activation and repression, RNA processing, and DNA repair. For example, it methylates histone H4 at arginine 3 (H4R3me2a) to create epigenetic marks that prevent heterochromatin spread and facilitate transcription, and it modulates the function of key transcription factors (e.g., ERα, RUNX1) as well as proteins central to DNA damage checkpoint responses (e.g., MRE11, 53BP1). In addition, PRMT1 is responsible for the majority of asymmetric dimethylarginine formation, and its expression is frequently elevated in various cancers, suggesting a role as a critical regulator of fundamental cellular processes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn oncogenic contexts, PRMT1 exerts multifaceted roles by modulating transcriptional complexes and signaling cascades that promote malignant transformation, proliferation, and metastasis. It participates in oncogenic transcription complexes—such as those involving mixed lineage leukemia (MLL) fusions and AML1‐ETO—by depositing H4R3 methyl marks and altering co-regulator binding, thereby enhancing self-renewal of leukemic cells. Furthermore, PRMT1-mediated methylation of key proteins including RBM15, EGFR, Twist1, and BAD has been shown to regulate alternative RNA splicing, enhance receptor–ligand interactions and dimerization, drive epithelial–mesenchymal transition (EMT), and block pro-survival kinase phosphorylation. This diverse modulation is central to oncogenesis in cancers such as breast, lung, and acute myeloid leukemia, where even specific PRMT1 isoforms have been linked to altered cell invasion and survival. Moreover, PRMT1-dependent methylation of FLT3 in FLT3-ITD+ leukemia cells underscores its role in maintaining oncogenic signaling independent of kinase activity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in tumorigenesis, PRMT1 influences protein–protein interactions, subcellular localization and stress responses in both neuronal and viral settings. It methylates RNA-binding proteins such as FUS/TLS, FMRP, and EWS to regulate their nucleo–cytoplasmic shuttling and aggregation properties—events that are central to the pathogenesis of neurodegenerative diseases. In addition, PRMT1 modulates the activity of nuclear receptors like PXR and alters viral protein function via methylation of HBx and LANA, thereby affecting viral transcription and latency. Its activity also impacts mitochondrial Ca²⁺ uptake by methylating MICU1 and collaborates with cofactors (e.g., hCAF1) and stress granule components to fine-tune RNA metabolism. Such diverse regulatory functions highlight PRMT1’s importance in multiple cellular contexts, including maintenance of genomic stability and response to environmental stress"}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "22", "end_ref": "36"}]}, {"type": "t", "text": ">.\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, targeted inhibition studies in acute myeloid leukemia models further underscore the therapeutic potential of modulating PRMT1 activity to eradicate cancer cell survival pathways, with strategies combining PRMT1 inhibition alongside tyrosine kinase inhibitors showing promise for eliminating resistant leukemic clones."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "37"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Masanori Yoshimatsu, Gouji Toyokawa, Shinya Hayami, et al. 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