RGG-motif self-association regulates eIF4G-binding translation repressor protein Scd6

References

• Sonenberg N, Hinnebusch AG. New modes of translational control in development, behavior, and disease. Mol Cell. 2007;28:721–729.
   PubMed Web of Science ®Google Scholar
• Kronja I, Orr-Weaver TL. Translational regulation of the cell cycle: when, where, how and why? Philos Trans R Soc Lond B Biol Sci. 2011;366:3638–3652.
   PubMed Web of Science ®Google Scholar
• Tanenbaum ME, Stern-Ginossar N, Weissman JS, et al. Regulation of mRNA translation during mitosis. Elife. 2015;4:e07957.
   Web of Science ®Google Scholar
• Sonenberg N, Hinnebusch AG. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell. 2009;136:731–745.
   PubMed Web of Science ®Google Scholar
• Banerjee A, Ifrim MF, Valdez AN, et al. Aberrant RNA translation in fragile X syndrome: from FMRP mechanisms to emerging therapeutic strategies. Brain Res. 2018;1693:24–36.
   PubMed Web of Science ®Google Scholar
• Adeli K. Translational control mechanisms in metabolic regulation: critical role of RNA binding proteins, microRNAs, and cytoplasmic RNA granules. Am J Physiol Endocrinol Metab. 2011;301:E1051–1064.
   PubMed Web of Science ®Google Scholar
• Siddiqui N, Sonenberg N. Signalling to eIF4E in cancer. Biochem Soc Trans. 2015;43:763–772.
   PubMed Web of Science ®Google Scholar
• Hershey JW, Sonenberg N, Mathews MB. Principles of translational control: an overview. Cold Spring Harb Perspect Biol. 2012;4:a011528.
   Web of Science ®Google Scholar
• Jackson RJ, Hellen CU, Pestova TV. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol. 2010;11:113–127.
   PubMed Web of Science ®Google Scholar
• Kahvejian A, Svitkin YV, Sukarieh R, et al. Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms. Genes Dev. 2005;19:104–113.
   PubMed Web of Science ®Google Scholar
• Hinnebusch AG, Lorsch JR. The mechanism of eukaryotic translation initiation: new insights and challenges. Cold Spring Harb Perspect Biol. 2012;4:a011544.
   Web of Science ®Google Scholar
• Teleman AA, Chen YW, Cohen SM. 4E-BP functions as a metabolic brake used under stress conditions but not during normal growth. Genes Dev. 2005;19:1844–1848.
   PubMed Web of Science ®Google Scholar
• Gebauer F, Hentze MW. Molecular mechanisms of translational control. Nat Rev Mol Cell Biol. 2004;5:827–835.
   PubMed Web of Science ®Google Scholar
• Grzmil M, Hemmings BA. Translation regulation as a therapeutic target in cancer. Cancer Res. 2012;72:3891–3900.
   PubMed Web of Science ®Google Scholar
• Rajyaguru P, She M, Parker R. Scd6 targets eIF4G to repress translation: RGG motif proteins as a class of eIF4G-binding proteins. Mol Cell. 2012;45:244–254.
   PubMed Web of Science ®Google Scholar
• Hilliker A, Gao Z, Jankowsky E, et al. The DEAD-box protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex. Mol Cell. 2011;43:962–972.
   PubMed Web of Science ®Google Scholar
• Paquin N, Menade M, Poirier G, et al. Local activation of yeast ASH1 mRNA translation through phosphorylation of Khd1p by the casein kinase Yck1p. Mol Cell. 2007;26:795–809.
   PubMed Web of Science ®Google Scholar
• Anantharaman V, Aravind L. Novel conserved domains in proteins with predicted roles in eukaryotic cell-cycle regulation, decapping and RNA stability. BMC Genomics. 2004;5:45.
   PubMed Web of Science ®Google Scholar
• Thandapani P, O’Connor TR, Bailey TL, et al. Defining the RGG/RG motif. Mol Cell. 2013;50:613–623.
   PubMed Web of Science ®Google Scholar
• Poornima G, Shah S, Vignesh V, et al. Arginine methylation promotes translation repression activity of eIF4G-binding protein, Scd6. Nucleic Acids Res. 2016;44:9358–9368.
   PubMed Web of Science ®Google Scholar
• Roy D, Rajyaguru PI. Suppressor of clathrin deficiency (Scd6)-An emerging RGG-motif translation repressor. Wiley Interdiscip Rev RNA. 2018;9:e1479.
   PubMed Web of Science ®Google Scholar
• Xu J, Chua NH. Arabidopsis decapping 5 is required for mRNA decapping, P-body formation, and translational repression during postembryonic development. Plant Cell. 2009;21:3270–3279.
   PubMed Web of Science ®Google Scholar
• Yang WH, Yu JH, Gulick T, et al. RNA-associated protein 55 (RAP55) localizes to mRNA processing bodies and stress granules. Rna. 2006;12:547–554.
   PubMed Web of Science ®Google Scholar
• Tanaka KJ, Ogawa K, Takagi M, et al. RAP55, a cytoplasmic mRNP component, represses translation in Xenopus oocytes. J Biol Chem. 2006;281:40096–40106.
   PubMed Web of Science ®Google Scholar
• Matsumoto K, Nakayama H, Yoshimura M, et al. PRMT1 is required for RAP55 to localize to processing bodies. RNA Biol. 2012;9:610–623.
   PubMed Web of Science ®Google Scholar
• Mitchell SF, Walker SE, Algire MA, et al. The 5ʹ-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway. Mol Cell. 2010;39:950–962.
   PubMed Web of Science ®Google Scholar
• Meszaros B, Erdos G, Dosztanyi Z. IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding. Nucleic Acids Res. 2018;46:W329–W337.
   PubMed Web of Science ®Google Scholar
• Franzmann T, Alberti S. Prion-like low-complexity sequences: key regulators of protein solubility and phase behavior. J Biol Chem. 2018;294(18):7128–7136.
   PubMed Web of Science ®Google Scholar
• Decker CJ, Teixeira D, Parker R. Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae. J Cell Biol. 2007;179:437–449.
   PubMed Web of Science ®Google Scholar
• Buchan JR, Muhlrad D, Parker R. P bodies promote stress granule assembly in Saccharomyces cerevisiae. J Cell Biol. 2008;183:441–455.
   PubMed Web of Science ®Google Scholar
• Segal SP, Dunckley T, Parker R. Sbp1p affects translational repression and decapping in Saccharomyces cerevisiae. Mol Cell Biol. 2006;26:5120–5130.
   PubMed Web of Science ®Google Scholar
• Rajyaguru P, Parker R. RGG motif proteins: modulators of mRNA functional states. Cell Cycle. 2012;11:2594–2599.
   PubMed Web of Science ®Google Scholar
• Frankel A, Clarke S. RNase treatment of yeast and mammalian cell extracts affects in vitro substrate methylation by type I protein arginine N-methyltransferases. Biochem Biophys Res Commun. 1999;259:391–400.
   PubMed Web of Science ®Google Scholar
• Mitchell SF, Jain S, She M, et al. Global analysis of yeast mRNPs. Nat Struct Mol Biol. 2013;20:127–133.
   PubMed Web of Science ®Google Scholar
• Chong PA, Vernon RM, Forman-Kay JD. RGG/RG Motif Regions in RNA Binding and Phase Separation. J Mol Biol. 2018;430:4650–4665.
   PubMed Web of Science ®Google Scholar
• Michelitsch MD, Weissman JS. A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc Natl Acad Sci U S A. 2000;97:11910–11915.
   PubMed Web of Science ®Google Scholar
• Shaw DJ, Morse R, Todd AG, et al. Identification of a self-association domain in the Ewing’s sarcoma protein: a novel function for arginine-glycine-glycine rich motifs? J Biochem. 2010;147:885–893.
   PubMed Web of Science ®Google Scholar
• Ohno T, Rao VN, Reddy ES. EWS/Fli-1 chimeric protein is a transcriptional activator. Cancer Res. 1993;53:5859–5863.
   PubMed Web of Science ®Google Scholar
• Tritschler F, Eulalio A, Helms S, et al. Similar modes of interaction enable Trailer Hitch and EDC3 to associate with DCP1 and Me31B in distinct protein complexes. Mol Cell Biol. 2008;28:6695–6708.
   PubMed Web of Science ®Google Scholar
• Kruger T, Hofweber M, Kramer S. SCD6 induces ribonucleoprotein granule formation in trypanosomes in a translation-independent manner, regulated by its Lsm and RGG domains. Mol Biol Cell. 2013;24:2098–2111.
   PubMed Web of Science ®Google Scholar
• Vernon RM, Chong PA, Tsang B, et al. Pi-Pi contacts are an overlooked protein feature relevant to phase separation. Elife. 2018;7:e31486.
   Web of Science ®Google Scholar
• McBride AE, Cook JT, Stemmler EA, et al. Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions. J Biol Chem. 2005;280:30888–30898.
   PubMed Web of Science ®Google Scholar
• Ryan VH, Dignon GL, Zerze GH, et al. Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation. Mol Cell. 2018;69:465–479 e467.
   PubMed Web of Science ®Google Scholar
• Hofweber M, Hutten S, Bourgeois B, et al. Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation. Cell. 2018;173:706–719 e713.
   PubMed Web of Science ®Google Scholar
• Tsai WC, Gayatri S, Reineke LC, et al. Arginine Demethylation of G3BP1 Promotes Stress Granule Assembly. J Biol Chem. 2016;291:22671–22685.
   PubMed Web of Science ®Google Scholar
• Arribas-Layton M, Dennis J, Bennett EJ, et al. The C-Terminal RGG Domain of Human Lsm4 Promotes Processing Body Formation Stimulated by Arginine Dimethylation. Mol Cell Biol. 2016;36:2226–2235.
   PubMed Web of Science ®Google Scholar