ArticleNucleic acids research2020
RPS28B mRNA acts as a scaffold promoting cis-translational interaction of proteins driving P-body assembly.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 31 citations in OpenAlex.
- P-bodies act as dynamic control hubs for RNA processing and storage.The Journal of biological chemistry · 2026Article
- Investigating the role of RNA-binding protein Ssd1 in aneuploidy tolerance through network analysis.RNA (New York, N.Y.) · 2024Article
- Quantifying 3'UTR length from scRNA-seq data reveals changes independent of gene expression.Nature communications · 2024Article
- Proteins rather than mRNAs regulate nucleation and persistence of Oskar germ granules in Drosophila.Cell reports · 2023Article
- The Labyrinthine Landscape of APP Processing: State of the Art and Possible Novel Soluble APP-Related Molecular Players in Traumatic Brain Injury and Neurodegeneration.International journal of molecular sciences · 2023Article
- Structural and functional organization of germ plasm condensates.The Biochemical journal · 2022Review
- Context-specific regulation and function of mRNA alternative polyadenylation.Nature reviews. Molecular cell biology · 2022Review
- Assay to Study the Phase-transition Behavior of Edc3, a Conserved Processing Body (P-body) Marker Protein.Bio-protocol · 2022Article
- Enhancers regulate 3' end processing activity to control expression of alternative 3'UTR isoforms.Nature communications · 2022Article
- Low complexity RGG-motif sequence is required for Processing body (P-body) disassembly.Nature communications · 2022Article
- A working model for condensate RNA-binding proteins as matchmakers for protein complex assembly.RNA (New York, N.Y.) · 2022Review
- It's Just a Phase: Exploring the Relationship Between mRNA, Biomolecular Condensates, and Translational Control.Frontiers in genetics · 2022Review
- Condensation of pericentrin proteins in human cells illuminates phase separation in centrosome assembly.Journal of cell science · 2021Article
- Article
- In vivo reconstitution finds multivalent RNA-RNA interactions as drivers of mesh-like condensates.eLife · 2021Article
- RNAs as Regulators of Cellular Matchmaking.Frontiers in molecular biosciences · 2021Review
- RNA Granules: A View from the RNA Perspective.Molecules (Basel, Switzerland) · 2020Review
- 3' UTRs Regulate Protein Functions by Providing a Nurturing Niche during Protein Synthesis.Cold Spring Harbor symposia on quantitative biology · 2019Article
- Stress granule and P-body clearance: Seeking coherence in acts of disappearance.Seminars in cell & developmental biologyReview
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
P-bodies (PBs) are cytoplasmic mRNA-protein (mRNP) granules conserved throughout eukaryotes which are implicated in the repression, storage and degradation of mRNAs. PB assembly is driven by proteins with self-interacting and low-complexity domains. Non-translating mRNA also stimulates PB assembly, however no studies to date have explored whether particular mRNA transcripts are more critical than others in facilitating PB assembly. Previous work revealed that rps28bΔ (small ribosomal subunit-28B) mutants do not form PBs under normal growth conditions. Here, we demonstrate that the RPS28B 3'UTR is important for PB assembly, consistent with it harboring a binding site for the PB assembly protein Edc3. However, expression of the RPS28B 3'UTR alone is insufficient to drive PB assembly. Intriguingly, chimeric mRNA studies revealed that Rps28 protein, translated in cis from an mRNA bearing the RPS28B 3'UTR, physically interacts more strongly with Edc3 than Rps28 protein synthesized in trans. This Edc3-Rps28 interaction in turn facilitates PB assembly. Our work indicates that PB assembly may be nucleated by specific RNA 'scaffolds'. Furthermore, this is the first description in yeast to our knowledge of a cis-translated protein interacting with another protein in the 3'UTR of the mRNA which encoded it, which in turn stimulates assembly of cellular structures.
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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.