Arginine Methylation, Ubiquitination Shape Cancer

A review published in Genes & Diseases highlights the complex interplay between protein arginine methylation and ubiquitination, two forms of protein modification that can profoundly influence cancer development, progression and treatment response. The article brings together current understanding of how these interconnected molecular processes regulate proteins involved in cancer and identifies opportunities for future therapeutic approaches.

Protein arginine methyltransferases (PRMTs) modify arginine residues in histone and nonhistone proteins, influencing protein activity, interactions and cellular functions. Ubiquitination, meanwhile, can control the stability and activity of proteins by attaching ubiquitin molecules to selected targets. Rather than operating independently, these systems form a dynamic, bidirectional network in which methylation can alter ubiquitination and protein degradation, while ubiquitination can regulate the stability and activity of PRMT enzymes.