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- W2509062642 abstract "Stress granules (SGs) are cytoplasmic condensates of stalled messenger ribonucleoprotein complexes (mRNPs) that form when eukaryotic cells encounter environmental stress. RNA-binding proteins are enriched for arginine methylation and facilitate SG assembly through interactions involving regions of low amino acid complexity. How methylation of specific RNA-binding proteins regulates RNA granule assembly has not been characterized. Here, we examined the potent SG-nucleating protein Ras-GAP SH3-binding protein 1 (G3BP1), and found that G3BP1 is differentially methylated on specific arginine residues by protein arginine methyltransferase (PRMT) 1 and PRMT5 in its RGG domain. Several genetic and biochemical interventions that increased methylation repressed SG assembly, whereas interventions that decreased methylation promoted SG assembly. Arsenite stress quickly and reversibly decreased asymmetric arginine methylation on G3BP1. These data indicate that arginine methylation in the RGG domain prevents large SG assembly and rapid demethylation is a novel signal that regulates SG formation." @default.
- W2509062642 created "2016-09-16" @default.
- W2509062642 creator A5001008905 @default.
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- W2509062642 creator A5017825556 @default.
- W2509062642 creator A5028722054 @default.
- W2509062642 creator A5069369344 @default.
- W2509062642 date "2016-10-01" @default.
- W2509062642 modified "2023-10-14" @default.
- W2509062642 title "Arginine Demethylation of G3BP1 Promotes Stress Granule Assembly" @default.
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- W2509062642 doi "https://doi.org/10.1074/jbc.m116.739573" @default.
- W2509062642 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5077203" @default.
- W2509062642 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27601476" @default.
- W2509062642 hasPublicationYear "2016" @default.
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