Dual role of PRMT1-dependent arginine methylation in cellular responses to genotoxic stress

Abstract

We have recently shown that arginine methylation by protein arginine N-methyltransferase 1 (PRMT1) controls the response to cisplatin in ovarian cancer cells. In addition to increased methylation of chromatin proteins that favors senescence-associated secretory phenotype (SASP) activation, our study unraveled global hypo-methylation of RNA-binding proteins, which – we speculate – may promote their phase separation and stress granules formation.

Keywords

• arginine methylation
• mass spectrometry-based proteomics
• prmt1
• sasp
• cisplatin
• stress granules
• llps
• phosphorylation