PRMT5
- Known as:
- PRMT5
- Catalog number:
- Y214157
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- PRMT5
Related genes to: PRMT5
- Gene:
- PRMT5 NIH gene
- Name:
- protein arginine methyltransferase 5
- Previous symbol:
- HRMT1L5, SKB1
- Synonyms:
- SKB1Hs
- Chromosome:
- 14q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-06-18
- Date modifiied:
- 2017-12-15
Related products to: PRMT5
Related articles to: PRMT5
- Conventional chondrosarcoma (cCS) is a malignant bone tumor with intrinsic resistance to cytotoxic therapy. Advances in genomic profiling have revealed recurrent alterations that are redefining the therapeutic landscape for these tumors. - Source: PubMed
Publication date: 2026/09/20
Torrado CarlosConley Anthony P - Protein arginine methyltransferases (PRMTs) constitute a family of nine enzymes that catalyze the post-translational methylation of arginine residues on histone and non-histone proteins. This epigenetic modification regulates diverse cellular processes including gene transcription, RNA splicing, signal transduction, and protein-protein interactions. Emerging evidence indicates that dysregulated PRMT activity contributes significantly to the pathogenesis of cardiovascular diseases (CVDs), including atherosclerosis, hypertension, heart failure, and myocardial infarction. This review synthesizes current literature on PRMT-mediated mechanisms in cardiovascular pathology, examining the roles of individual PRMT isoforms, their downstream substrates, and the therapeutic implications of PRMT modulation. PRMT1, PRMT5, and PRMT7 demonstrate cardioprotective functions under physiological conditions but contribute to pathological remodeling when dysregulated. The PRMT-DDAH-ADMA axis emerges as a critical regulator of endothelial nitric oxide pro-duction and vascular homeostasis. Type I PRMTs generate asymmetric dimethylarginine (ADMA), an endogenous nitric oxide synthase inhibitor that promotes endothelial dysfunction and atherosclerosis. Type II PRMTs, particularly PRMT5, regulate cardiac fibroblast activation, hypertrophic signaling, and vascular smooth muscle cell phenotypic switching. PRMTs represent promising therapeutic targets for cardiovascular disease intervention. Selective PRMT inhibitors have demonstrated efficacy in preclinical models of cardiac hypertrophy, fibrosis, and ischemic injury. Future research should focus on developing isoform-specific inhibitors with favorable safety profiles and establishing biomarker-guided patient selection strategies for PRMT-targeted therapies. - Source: PubMed
Publication date: 2026/09/01
Zhang TingLei HongZhang Chunmei - The efficacy of immune checkpoint blockade in triple-negative breast cancer (TNBC) is limited by poor CD8⁺ T cell infiltration. Here, we demonstrate that tumor-derived proprotein convertase subtilisin/kexin type 9 (PCSK9) drives CD8⁺ T cell exclusion, and we identify protein arginine methyltransferase 5 (PRMT5) as an important epigenetic regulator responsible for PCSK9 expression in TNBC. Mechanistically, we elucidate that PRMT5-mediated methylation of the chromobox homolog 8 (CBX8) facilitates its interaction with the deubiquitinase USP7, which removes K33-linked ubiquitination on CBX8. This post-translational modification modulates CBX8 function, enabling it to drive the transcriptional upregulation of key downstream targets PCSK9, which inhibits CD8 T cell infiltration, and LGR5, which enhances tumor stemness. Crucially, inhibition of PRMT5 profoundly sensitizes TNBC tumors to anti-PD-1 therapy in vivo. Our work unveils a novel epigenetic pathway orchestrated by PRMT5 that converges on the functional modulation of CBX8 to synchronously governs CD8⁺ T cell exclusion and tumor stemness, nominating PRMT5 inhibition as a compelling therapeutic strategy for combination immunotherapy in TNBC. - Source: PubMed
Publication date: 2026/09/14
Chen CongcongZhang YuhengLiu ChangZhao RunkaiLiu KaimingGuo ZhiqiYang YinyinWang CongTian JiaxinGuo YanguanChen GuoJin LiyanZhu XunZhou DanyangJiang Guoqin - Protein arginine methyltransferase 5 (PRMT5) is overexpressed in many cancers and correlates with poor patient survival. In prostate cancer, PRMT5 cooperates with its cofactor pICln to promote tumour growth by epigenetically activating androgen receptor (AR) expression. Using a near-atomic cryo-EM structure of PRMT5/MEP50/pICln complex, we identified a previously undefined, pICln-specific protein-protein interaction (PPI) interface on PRMT5, termed P4I. Structure-based virtual screening identified the FDA-approved compound etravirine as a binder to this site. BiFC, Co-IP, and PLA assays confirmed that etravirine disrupts PRMT5/pICln interaction. A cryo-EM structure of PRMT5/MEP50/etravirine further validated on-target binding at P4I. Functionally, etravirine reduced prostate cancer cell proliferation, inhibited tumour growth, and downregulated AR and AR-V7 expression in cells and in mouse models. These results demonstrate that the unique P4I interface is a promising therapeutic target and that etravirine serves as a proof-of-concept lead compound for exploring the potential of P4I-targeted strategies in prostate cancer. - Source: PubMed
Publication date: 2026/09/08
Chi ZhixiaXu XueyongShen ZhihangDeng XuehongElzey Bennett DLi ChenglongJiang WenHu Chang-Deng - Loss of methylthioadenosine phosphorylase (MTAP), which occurs in approximately 10-15% of non-small-cell lung cancers and other solid tumors, represents a key synthetic-lethal vulnerability linking tumor metabolism to epigenetic regulation. MTAP deletion disrupts the methionine salvage pathway, leading to accumulation of methylthioadenosine (MTA) and selective dependence on protein arginine methyltransferase 5 (PRMT5). This metabolic rewiring provides a unique therapeutic opportunity to target the MAT2A-PRMT5 axis. This review summarizes recent advances in understanding MTAP biology, including the PRMT5/MAT2A feedback network, tumor heterogeneity, and adaptive resistance mechanisms encompassing metabolic compensation, splicing plasticity, and immune-cold microenvironments associated with 9p21 co-deletion. Emerging clinical data on MTA-cooperative PRMT5 inhibitors and MAT2A inhibitors are discussed, alongside challenges in diagnostic accuracy, biomarker validation, and patient stratification. Despite encouraging early-phase activity, the translation of MTAP-directed therapy is constrained by diagnostic discordance, tumor adaptability, and the absence of prospective, biomarker-driven trials. Future progress will depend on harmonized detection methods, integration of metabolic biomarkers, and rational therapeutic combinations with targeted or immune-based approaches. Collectively, targeting the MTAP-MAT2A-PRMT5 axis exemplifies a metabolism-informed precision-oncology strategy with significant translational potential. - Source: PubMed
Publication date: 2026/08/29
Arter Zhaohui LiaoShim Joo Sung GabrielPark CathleenWaliany SarahLim Sun MinSoo Ross A