ArticleThe EMBO journal2011
Smaug assembles an ATP-dependent stable complex repressing nanos mRNA translation at multiple levels.
Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
49 citing papers in PubMed, 87 citations in OpenAlex.
- Article
- Review
- RNA-binding protein SAMD4A targets FGF2 to regulate cardiomyocyte lineage specification from human embryonic stem cells.Stem cell research & therapy · 2025Article
- Article
- How germ granules promote germ cell fate.Nature reviews. Genetics · 2024Review
- Direct observation of translational activation by a ribonucleoprotein granule.Nature cell biology · 2024Article
- Me31B: a key repressor in germline regulation and beyond.Bioscience reports · 2024Review
- P-body-like condensates in the germline.Seminars in cell & developmental biology · 2024Review
- Structural basis for binding ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Mutational analysis of the functional motifs of the DEAD-box RNA helicase Me31B/DDX6 in Drosophila germline development.FEBS letters · 2023Article
- RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system.Nucleic acids research · 2023Article
- Endoplasmic reticulum-associated protein degradation contributes to Toll innate immune defense inFrontiers in immunology · 2022Article
- me31B regulates stem cell homeostasis by preventing excess dedifferentiation in the Drosophila male germline.Journal of cell science · 2021Article
- A genome-wide transcriptomic analysis of embryos fathered by obese males in a murine model of diet-induced obesity.Scientific reports · 2021Article
- Elucidation of the RNA-granule inducing sodium azide stress response through transcriptome analysis.Genomics · 2020Article
- Regulation of the RNA-binding protein Smaug by the GPCR Smoothened via the kinase Fused.EMBO reports · 2020Article
- Establishment of 5'-3' interactions in mRNA independent of a continuous ribose-phosphate backbone.RNA (New York, N.Y.) · 2020Article
- The PIWI protein Aubergine recruits eIF3 to activate translation in the germ plasm.Cell research · 2020Article
- A Non-amyloid Prion Particle that Activates a Heritable Gene Expression Program.Molecular cell · 2020Article
- Expression Analysis of mRNA Decay of Maternal Genes duringInternational journal of molecular sciences · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nanos (nos) mRNA encodes the posterior determinant of the Drosophila embryo. Translation of the RNA is repressed throughout most of the embryo by the protein Smaug binding to Smaug recognition elements (SREs) in the 3' UTR. Translation is locally activated at the posterior pole by Oskar. This paper reports that the SREs govern the time- and ATP-dependent assembly of an exceedingly stable repressed ribonucleoprotein particle (RNP) in embryo extract. Repression can be virtually complete. Smaug and its co-repressor Cup as well as Trailer hitch and the DEAD box protein Me31B are part of the repressed RNP. The initiation factor eIF4G is specifically displaced, and 48S pre-initiation complex formation is inhibited. However, later steps in translation initiation are also sensitive to SRE-dependent inhibition. These data confirm several previously untested predictions of a current model for Cup-dependent repression but also suggest that the Cup model by itself is insufficient to explain translational repression of the nos RNA. In the embryo extract, recombinant Oskar relieves translational repression and deadenylation by preventing Smaug's binding to the SREs.
Indexed as
Identifiers
What OpenQuestion holds
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.