ArticleNucleic acids research2016
Arginine methylation promotes translation repression activity of eIF4G-binding protein, Scd6.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 46 citations in OpenAlex.
- RGG-motif protein Scd6 affects oxidative stress response by regulating cytosolic caTalase T1 (Ctt1).RNA biology · 2026Article
- Arginine methylation-dependent stabilization of SUV39H1 promotes breast cancer growth.Oncogene · 2026Article
- Dual inhibition of PRMT1 and SUV39H1 suppresses breast cancer progression and enhances immunotherapy response.International journal of biological sciences · 2026Article
- Phase separation is regulated by post-translational modifications and participates in the developments of human diseases.Heliyon · 2024Review
- Tyrosine phosphorylation of CARM1 promotes its enzymatic activity and alters its target specificity.Nature communications · 2024Article
- The nexus between RNA-binding proteins and their effectors.Nature reviews. Genetics · 2023Review
- Assay to Study the Phase-transition Behavior of Edc3, a Conserved Processing Body (P-body) Marker Protein.Bio-protocol · 2022Article
- Low complexity RGG-motif sequence is required for Processing body (P-body) disassembly.Nature communications · 2022Article
- The Novel Protease Activities of JMJD5-JMJD6-JMJD7 and Arginine Methylation Activities of Arginine Methyltransferases Are Likely Coupled.Biomolecules · 2022Review
- The RNA Helicase Ded1 Regulates Translation and Granule Formation during Multiple Phases of Cellular Stress Responses.Molecular and cellular biology · 2022Article
- eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly.Frontiers in molecular biosciences · 2022Article
- Article
- PRMT1-dependent regulation of RNA metabolism and DNA damage response sustains pancreatic ductal adenocarcinoma.Nature communications · 2021Article
- Methylated HNRNPK acts on RPS19 to regulate ALOX15 synthesis in erythropoiesis.Nucleic acids research · 2021Article
- Analysis of the TORC1 interactome reveals a spatially distinct function of TORC1 in mRNP complexes.The Journal of cell biology · 2021Article
- Elucidation of the RNA-granule inducing sodium azide stress response through transcriptome analysis.Genomics · 2020Article
- Arginine methylation augments Sbp1 function in translation repression and decapping.The FEBS journal · 2019Article
- Psp2, a novel regulator of autophagy that promotes autophagy-related protein translation.Cell research · 2019Article
- The regulation, functions and clinical relevance of arginine methylation.Nature reviews. Molecular cell biology · 2019Review
- Experimental evolution reveals a general role for the methyltransferase Hmt1 in noise buffering.PLoS biology · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Regulation of translation plays a critical role in determining mRNA fate. A new role was recently reported for a subset of RGG-motif proteins in repressing translation initiation by binding eIF4G1. However the signaling mechanism(s) that leads to spatial and temporal regulation of repression activity of RGG-motif proteins remains unknown. Here we report the role of arginine methylation in regulation of repression activity of Scd6, a conserved RGG-motif protein. We demonstrate that Scd6 gets arginine methylated at its RGG-motif and Hmt1 plays an important role in its methylation. We identify specific methylated arginine residues in the Scd6 RGG-motif in vivo We provide evidence that methylation augments Scd6 repression activity. Arginine methylation defective (AMD) mutant of Scd6 rescues the growth defect caused by overexpression of Scd6, a feature of translation repressors in general. Live-cell imaging of the AMD mutant revealed that it is defective in inducing formation of stress granules. Live-cell imaging and pull-down results indicate that it fails to bind eIF4G1 efficiently. Consistent with these results, a strain lacking Hmt1 is also defective in Scd6-eIF4G1 interaction. Our results establish that arginine methylation augments Scd6 repression activity by promoting eIF4G1-binding. We propose that arginine methylation of translation repressors with RGG-motif could be a general modulator of their repression activity.
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