ArticleRNA biology2019
RGG-motif self-association regulates eIF4G-binding translation repressor protein Scd6.
Article in RNA biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- RGG-motif protein Scd6 affects oxidative stress response by regulating cytosolic caTalase T1 (Ctt1).RNA biology · 2026Article
- Phase separation of PGL-3 driven by structured domains that oligomerize and interact with RGG motifs.EMBO reports · 2026Article
- Phase separation is regulated by post-translational modifications and participates in the developments of human diseases.Heliyon · 2024Review
- The RGG motif proteins: Interactions, functions, and regulations.Wiley interdisciplinary reviews. RNA · 2023Review
- Type I arginine methyltransferases are intervention points to unveil the oncogenic Epstein-Barr virus to the immune system.Nucleic acids research · 2022Article
- Discovering molecular features of intrinsically disordered regions by using evolution for contrastive learning.PLoS computational biology · 2022Article
- Article
- Arginine methylation augments Sbp1 function in translation repression and decapping.The FEBS journal · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Regulation of mRNA translation plays a key role in the control of gene expression. Scd6, a conserved RGG-motif containing protein represses translation by binding to translation initiation factor eIF4G1. Here we report that Scd6 binds itself in RGG-motif dependent manner and self-association regulates its repression activity. Scd6 self-interaction competes with eIF4G1 binding and methylation of Scd6 RGG-motif by Hmt1 negatively affects self-association. Results pertaining to Sbp1 indicate that self-association could be a general feature of RGG-motif containing translation repressor proteins. Taken together, our study reveals a mechanism of regulation of eIF4G-binding RGG-motif translation repressors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.