Ask about this productRelated genes to: PRMT3 antibody
- Gene:
- PRMT3 NIH gene
- Name:
- protein arginine methyltransferase 3
- Previous symbol:
- HRMT1L3
- Synonyms:
- -
- Chromosome:
- 11p15.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-06-18
- Date modifiied:
- 2014-11-19
Related products to: PRMT3 antibody
Related articles to: PRMT3 antibody
- Porcine epidemic diarrhea virus (PEDV) represents a severe threat to the global swine industry. Its infection process involves intricate virus-host interactions and immune evasion mechanisms, but effective therapeutic targets remain elusive. In this study, we identified protein arginine methyltransferase 3 (PRMT3) as a novel regulatory factor that significantly modulates PEDV infection via genome-wide CRISPR/Cas9 knockout library screening. Knockout or inhibition of PRMT3 markedly enhanced PEDV infection in multiple cell lines, including LLC-PK1, IPEC-J2, and primary porcine intestinal epithelial cells. Mechanistic investigations revealed that PRMT3 can restrict PEDV infection by interacting with vesicle-associated membrane protein-associated protein A (VAPA). Further analysis revealed that VAPA facilitates cholesterol transport through binding to oxysterol-binding protein (OSBP) and inhibits the autophagic degradation of the viral nucleocapsid (N) protein, with both processes being critical for promoting PEDV infection in host cells. A detailed analysis revealed that K52 within its major sperm protein (MSP) domain interacts with D404 and D405 in the two phenylalanines in an acidic tract (FFAT)-like motifs of the N protein, and these interactions proved essential for PEDV infection. In summary, this is the first study to identify and validate the PRMT3-VAPA-N protein autophagic degradation axis as a key pathway through which PRMT3 suppresses PEDV infection, with VAPA acting as an essential host factor for PEDV pathogenesis. These findings uncover novel signaling pathways and molecular targets for the development of anti-PEDV therapeutics. - Source: PubMed
Publication date: 2026/09/08
Wu He-YongZhong Shu-YuQi Ao-SiWang Zi-RuTu Qiu-SeLi FengWu RuiWang Jing-YaoSong FanZhang Tian-YiLi TingYu Qing-ChunYuan Hong-MingLv Dong-MeiOuyang Hong-ShengDu Xi-LiangPang Da-XinXie Zi-Cong - Loss or lack tumor immunogenicity promotes immune escape and resistance to immunotherapy. Arginine methylation, a key protein post-translational modification, participates in tumor progression and therapy resistance. However, whether arginine methylation directly influences the tumor immunogenicity and thereby modulates antitumor immune responses remains poorly understood. Here, we report that protein arginine methyltransferase 3 (PRMT3) exhibited a significantly negative association with antitumor immune signatures and survival outcomes in multiple cancers. Tumor-intrinsic PRMT3 deletion markedly delays tumor growth by promoting CD8 T cell infiltration and functional activation through the modulation of type I interferon (IFN) signaling. Mechanistically, PRMT3 catalyzes arginine asymmetric-dimethylation at the conserved Arg364 residue of cGAS, suppressing its capacity to activate the downstream STING signaling, which ultimately affects the tumor immunogenicity and overall antitumor immune responses. Combining PRMT3 deletion or pharmacological inhibition with anti-PD-1 antibody therapy achieved profoundly synergistic tumor control and elicited tumor-specific immunological memory. Collectively, our findings delineate a critical regulatory role of PRMT3 on tumor-intrinsic cGAS-mediated adaptive immunity, proposing immunogenicity-enhanced cancer treatment as a transformative strategy to achieve potentiated antitumor efficacy. - Source: PubMed
Publication date: 2026/08/25
Chen YuLiu YangPeng JianfengWang XiaolongWei ZhonghuiYin XiaoyanZhai XueyingLi YankangYu JinmingMeng Xiangjiao - Protein arginine methyltransferase 3 (PRMT3) is a type I arginine methyltransferase that catalyzes asymmetric dimethylation of arginine residues on diverse substrate proteins. Initially characterized as a regulator of ribosomal protein methylation, PRMT3 has more recently been implicated in several cancer-related processes. Accumulating evidence suggests that PRMT3 is dysregulated in a variety of malignancies, including hepatocellular carcinoma, colorectal cancer, glioblastoma, breast cancer, pancreatic cancer, and non-small cell lung cancer. Through arginine methylation of selected regulatory proteins, PRMT3 has been linked to signaling pathways associated with tumor progression, metabolic adaptation, immune modulation, and therapeutic resistance. Mechanistically, available studies indicate that PRMT3 can regulate RNA-associated networks by methylating RNA-binding proteins and epitranscriptomic regulators such as IGF2BP1 and METTL14, thereby influencing mRNA stability and gene expression programs. In addition, PRMT3 has been reported to contribute to tumor metabolic reprogramming by promoting glycolytic activity and modulating amino acid metabolism through factors including HIF1A, PDHK1, and IDO1. These alterations may support tumor growth and, in some contexts, influence the tumor immune microenvironment. PRMT3 has also been associated with immune evasion, for example through effects on PD-L1 expression and innate immune signaling pathways such as cGAS-STING. Moreover, emerging evidence links PRMT3 to therapeutic resistance through mechanisms involving oncogenic transcript stabilization, immunometabolic remodeling, and drug efflux regulation. In this review, we summarize the current understanding of PRMT3 structure, catalytic mechanisms, and biological functions in cancer. We further discuss its emerging roles in metabolic regulation, immune suppression, and therapy resistance, while distinguishing mechanisms directly supported within specific cancer contexts from broader conceptual models inferred across studies. Overall, current evidence supports PRMT3 as an emerging and context-dependent regulator of tumor biology and a potential target for anticancer therapy. - Source: PubMed
Publication date: 2026/05/01
Jin HuiHuang HuaPan Xin - Protein arginine methyltransferase 3 (PRMT3) is a key member of the PRMT family that catalyzes the arginine methylation of proteins, thereby modulating their structure, localization, or interactions and influencing essential physiological processes, such as cell growth and signal transduction. Its dysregulation is closely associated with tumorigenesis and neurological disorders. PRMT3 is critically involved in cellular processes, such as cell growth, invasion, and apoptosis, making it a promising target for drug discovery. In this review, we summarized the structure and biological functions of PRMT3, particularly the mechanism of action in human diseases. We also evaluated the co-crystal structure of PRMT3 inhibitors. Furthermore, we examined the recent advancements in the development of PRMT3 modulators, including isoform-selective and partially isoform-selective PRMT3 inhibitors as well as PRMT3-targeting PROTACs, from a rational design perspective. Finally, we discussed the existing challenges and future directions in PRMT3-targeted drug discovery. - Source: PubMed
Publication date: 2026/02/04
Yu DongminHe KangMai CunjunLi Meifang - Protein arginine methyltransferases are key epigenetic regulators and promising targets for cancer therapy. PRMT4 plays an important role in transcriptional regulation and tumor progression, yet selective inhibition remains challenging because type I PRMTs share highly conserved catalytic sites. The success of allosteric inhibitors targeting PRMT3 and PRMT6 suggests that selective modulation through regulatory sites outside the catalytic pocket may also be feasible for PRMT4. Motivated by this rationale, we investigated whether PRMT4 undergoes conformational transitions between active and inactive states and whether it contains allosterically targetable pockets capable of regulating its enzymatic activity. Using an integrated computational strategy, we characterized the conformational dynamics and allosteric regulation mechanisms of PRMT4. Structural analysis identified a molecular switch involving order and disorder transitions of the N terminal helices that governs the active inactive transition. Free energy landscape analysis supported that this transition is thermodynamically accessible. We identified a PRMT3 like allosteric pocket, Cavity 1, whose targeting is predicted to disrupt inter chain communication and impair cofactor binding and active site organization. Dynamic residue network analysis further supported Cavity 1 as a functional allosteric site. We also identified a PRMT4 specific pocket, Cavity 2, with a distinct selectivity profile. These findings validate the active inactive switch and identify two druggable allosteric sites. Although experimental validation is required, this work provides a computational framework for the rational design of PRMT4 selective allosteric inhibitors. - Source: PubMed
Publication date: 2026/03/26
Abbas AmrMiao ZhanpengJin JiaYe Fei