Inhibition of type I PRMTs increases the proliferation capabilities of MuSCs with altered cellular metabolism, while maintaining their stem-like properties such as self-renewal and engraftment potential.

Biochemical, transcriptomic, and proteomic analyses reveal that protein arginine methyltransferases post-transcriptionally regulate intron detention—introns that persist in nuclear polyadenylated RNA—through methylation of RNA splicing and processing factors.

PRMT7-mediated SHANK2 methylation regulates breast cancer metastasis by activating endosomal FAK signals, and may provide potential clues for tumour metastasis treatment strategies.

Inhibiting PRMT1 enzymatic activity promotes megakaryocyte terminal differentiation via RBM15-mediated RNA metabolism, which is dysregulated in hematological malignancies.

The PRMT1 protein mediates arginine methylation of KCNQ2 channels to control neuronal excitability.

The transcription factor ERG recruits the PRMT5 enzyme to methylate the androgen receptor, presenting a post-translational regulatory mechanism that could be therapeutically exploited to control cell proliferation.

PRMT5 participates in ovarian granulosa cell lineage maintenance by regulating Wt1 IRES-dependent translation.

A chemical probe was characterized for potency, selectivity, and ability to alter CARM1-dependent epigenetic plasticity against cancer cell invasion.