Research ResourcePosttranslational Modifications

Proteome-wide analysis of arginine monomethylation reveals widespread occurrence in human cells

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Science Signaling  30 Aug 2016:
Vol. 9, Issue 443, pp. rs9
DOI: 10.1126/scisignal.aaf7329

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Appreciating arginine methylation

Posttranslational modifications, such as phosphorylation and ubiquitylation, regulate protein abundance, localization, interactions, and function. Larsen et al. investigated the landscape and functional roles of the posttranslational modification arginine methylation. RNA interference and high-throughput single-cell imaging revealed that arginine methylation regulated two proteins involved in RNA processing and transport. Arginine methylation by distinct arginine methyltransferases controlled the localization and RNA binding functions of the pre-mRNA splicing factor SRSF2 and the RNA-transporting activity of the protein HNRNPUL1. On a broader level, their data provide a rich resource for the future investigation of the function of arginine methylation and indicate that sites modified by this posttranslational modification are hotspots for mutations in disease.

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