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• W1562860130 endingPage "103" @default.
• W1562860130 startingPage "51" @default.
• W1562860130 abstract "Methylation of arginine residues within proteins results in a more subtle change than phosphorylation, but one that also has profound impacts on eukaryotic organisms. The rapidly expanding list of protein arginine methyltransferases (PRMTs) and PRMT substrates has implicated arginine methylation in a wide variety of cellular processes. This chapter explores the diverse functions of PRMTs by examining evidence for effects of arginine methylation and PRMTs on specific cellular processes, and connecting the data to molecular mechanisms that have been proposed to explain these effects. First, effects of arginine methylation on intermolecular interactions are addressed, focusing on how methylation affects protein-nucleic acid and protein-protein interactions. Next, the numerous linksamong PRMTs, arginine methylation, and cellular processes are described, including roles of PRMTs and methylation in transcription, cell signaling, protein transport, pre-mRNA splicing, ribosome assembly, and DNA damage repair. Finally, the broader implications of arginine methylation are considered by examining the connections between PRMTs and their substrates and development, differentiation, and disease." @default.
• W1562860130 created "2016-06-24" @default.
• W1562860130 creator A5032448027 @default.
• W1562860130 date "2006-01-01" @default.
• W1562860130 modified "2023-10-14" @default.
• W1562860130 title "3 Diverse roles of protein arginine methyltransferases" @default.
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