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PRMTs in Epigenetics and Disease

Protein arginine methyltransferases (PRMTs) are a family of enzymes that catalyze arginine methylation, a key post-translational modification involved in the regulation of gene expression, RNA processing, DNA repair, and signal transduction. PRMTs transfer methyl groups from S-adenosyl-L-methionine (SAM) to arginine residues on both histone and non-histone proteins, thereby modulating protein–protein interactions, subcellular localization, and protein activity.

 
Protein / Family Epigenetic Function Disease Association Key Publications Key Products
AKT Methylation by PRMT1 can alter transcription factor accessibility and AKT-dependent signaling Hormonone driven cancers, insulin resistance and metabolic disorders Yin et al., Nat. Commun. 2021.
BPTF Interacts indirectly with PRMTs by recognizing methylated histones generated by PRMTs such as PRMT1 (H4R3me2a) and PRMT6 (H3R2me2a) Cancer (neuroblastoma, breast cancer) and developmental disorders Fulton et al., J. Biol. Chem. 2018
BRCA1 PRMT1 methylates BRCA1 at specific arginine residues. Methylation regulates BRCA1’s DNA repair function, protein–protein interactions, and localization. Breast and ovarian cancers Montenegro et al., Sci. Rep. 2020.
MEP50 Essential for PRMT5-mediated symmetric arginine methylation on histones (H4R3me2s, H3R8me2s) and non-histone proteins Cancer progression, particularly in breast, lung, and prostate cancers Antonysamy et al., PNAS. 2012
MYC PRMTs, especially CARM1/PRMT4 and PRMT1, methylate MYC directly or methylate associated histones and coactivators. This modulates MYC’s transcriptional activity, chromatin recruitment, and protein stability. Transcription factor regulating cell proliferation, metabolism, ribosome biogenesis, and apoptosis. Liu et al., thno. 2020
NFKB PRMTs, particularly PRMT1 and CARM1/PRMT4, regulate NF-κB signaling by methylating NF-κB subunits (e.g., p65/RelA) or histones at NF-κB target genes. This affects transcriptional activity, nuclear localization, and cofactor recruitment. Transcription factor controlling inflammation, immune responses, cell survival, and proliferation. Ganesh et al., MCB. 2023
p53 Several PRMTs, including PRMT1, CARM1/PRMT4, and PRMT5, methylate p53 at specific arginine residues. Methylation modulates p53’s DNA binding, transcriptional activity, and protein stability. Transcription factor regulating cell cycle arrest, apoptosis, DNA repair, and senescence. Liu et al., Life. 2021
Type 1 PRMTs (PRMT1-4, PRMT6, PRMT 8) Generate asymmetric dimethylarginine (ADMA). Regulates transcription, nuclear receptor signaling, ribosomal protein methylation Multiple cancers (prostate,breast, lung), hormone related (via coactivator activity), and neurological disorders Luo et al., MedComm. 2025
Type II PRMTs (PRMT5, PRMT9) Generate symmetric dimethylarginine (SDMA), transcriptional repression, spicing factor methylation, Lymphoid cancers Schneider et al., SciDirect. 2025
Type III (PRMT7) Produces monomethylarginine (MMA), RNA processing and trascription regulation. Developmental disorders and tumor sensitivity to DNA-damaging agents. Ge et al., CBET. 2025.

 

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