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Suppressor of clathrin deficiency (Scd6)—An emerging RGG‐motif translation repressor

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Translation control plays a key role in variety of cellular processes. Translation initiation factors augment translation, whereas translation repressor proteins inhibit translation. Different repressors act by distinct mechanisms to accomplish the repression process. Although messenger RNAs (mRNAs) can be repressed at various steps of translation, most repressors have been reported to target the initiation step. We focus on one such translation repressor, an Arginine–Glycine–Glycine (RGG)‐motif containing protein Scd6. Using this protein as a model, we present a discourse on the known and possible functions of this repressor, its mechanism of action and its recently reported regulation. We suggest a case for conservation of the mechanism employed by Scd6 along with its regulation in orthologs, and propose that Scd6 family of proteins will be an ideal tool to understand translation control and mRNA fate decision mechanisms across biological systems. This article is categorized under: Translation > Translation Regulation RNA Turnover and Surveillance > Turnover/Surveillance Mechanisms RNA Interactions with Proteins and Other Molecules > RNA–Protein Complexes
Schematic representation of the conserved domain organization in the Scd6 family of proteins, using PROSITE (ExPASy). Peach colored ovals represent the Lsm domain, green triangles represent the FDF domain, and blue rectangles depict the RGG domain(s). Domain boundaries used to create this schematic have been shown in Table S1
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Regulation of Scd6 repression activity. Scd6 binds eIF4G1 via its RGG domain. The RGG domain gets arginine methylated predominantly by the methyltransferase Hmt1 at several arginines. Arginine methylation augments the binding of Scd6 to eIF4G1 consequently promoting translation repression
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Scd6 orthologs trailer hitch and CAR‐1 function in ER organization and secretion of proteins. In the absence of functional CAR‐1, the ER appears to be thick and dispersed throughout as compared to the well‐defined, reticulate state in wild type background. Proteins like Sar1 and Gurken are also mislocalized upon depletion of the Tral. ER is shown in light green, COPII vesicles in red, COPI vesicles in yellow, and Golgi in orange
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Multiple sequence alignment of the Scd6 family of proteins, using Clustal Omega. Domain demarcations are based on S. cerevisiae Scd6 sequence. The Lsm domain spans through amino acids residues 1–93 (blue line), linker region through 94–198 (yellow line), FDF domain through 199–282 (green line), and RGG domain through 283–349 (maroon line). The alignment shows the conserved N‐terminal hxG and C‐terminal +Gpph signatures of the Lsm domain. RNA‐binding motifs psppxpl, GTEx+ and pGp are also shown, with GTExR being highly conserved in Scd6 family. [h = hydrophobic; x = any residue; p = polar; l = aliphatic; s = small residue; (+) = positively charged amino acid; G = glycine; T = threonine; E = glutamic acid and R = arginine]. Arginine methylation modifications are denoted in ovals. Amino acid residues identified as only dimethylated are depicted in blue ovals, while those arginines reported to be both mono‐ and dimethylated are shown in red ovals. Residues that have been predicted but their methylation status remains unknown are in gray. Modifications in arginines of only the RGG, RGX, or RG sequence have been shown. Phosphorylation sites identified in the orthologs have been represented by red rectangles
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Schematic of the comparative analysis of aromatic amino acids (a), and the QN residues (b) within the RGG domains of Scd6 family of proteins. Domain boundaries are as described in Table S1
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RNA Interactions with Proteins and Other Molecules > RNA–Protein Complexes
RNA Turnover and Surveillance > Turnover/Surveillance Mechanisms
Translation > Translation Regulation

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