ArticleNucleic acids research2020
Unique repression domains of Pumilio utilize deadenylation and decapping factors to accelerate destruction of target mRNAs.
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 38 papers.
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Who cites it
38 citing papers in PubMed, 56 citations in OpenAlex.
- Global Regulatory Functions of the Human CCR4-NOT Complex in mRNA Deadenylation and Decay.bioRxiv : the preprint server for biology · 2026Article
- Human pumilio proteins use fuzzy multivalent hydrophobic interactions to recruit the CCR4-NOT deadenylase complex to repress mRNAs.The Journal of biological chemistry · 2026Article
- Cytoplasmic poly-adenosine binding proteins modulate susceptibility of mRNAs to Pumilio-mediated decay.Nucleic acids research · 2026Article
- Phosphorylation-dependent tuning of mRNA deadenylation rates.Nature structural & molecular biology · 2026Article
- Stem cell regulation: conserved pluripotency, transcriptional, and metabolic networks in animals and plants.Frontiers in cell and developmental biology · 2026Review
- Human Pumilio proteins use fuzzy multivalent hydrophobic interactions to recruit the CCR4-NOT deadenylase complex to repress mRNAs.bioRxiv : the preprint server for biology · 2025Article
- Multivalent interactions with CCR4-NOT and PABPC1 determine mRNA repression efficiency by tristetraprolin.Nature communications · 2025Article
- Significant roles in RNA-binding for the amino-terminal regions of Drosophila Pumilio and Nanos.PLoS genetics · 2025Article
- The short conserved region-2 of LARP4 interacts with ribosome-associated RACK1 and promotes translation.Nucleic acids research · 2025Article
- A higher order PUF complex is central to regulation of C. elegans germline stem cells.Nature communications · 2025Article
- The TRIM-NHL RNA-binding protein Brain Tumor coordinately regulates expression of the glycolytic pathway and vacuolar ATPase complex.Nucleic acids research · 2024Article
- The short conserved region-2 of LARP4 interacts with ribosome-associated RACK1 and promotes translation.bioRxiv : the preprint server for biology · 2024Article
- Regulation of theRNA (New York, N.Y.) · 2024Article
- A higher order PUF complex is central to regulation ofbioRxiv : the preprint server for biology · 2024Article
- Chemi-Northern: a versatile chemiluminescent northern blot method for analysis and quantitation of RNA molecules.RNA (New York, N.Y.) · 2024Article
- PUF partner interactions at a conserved interface shape the RNA-binding landscape and cell fate in Caenorhabditis elegans.Developmental cell · 2024Article
- Review
- Measuring Poly-Adenosine Tail Length of RNAs by High-Resolution Northern Blotting Coupled with RNase H Cleavage.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Cell-type-specific interacting proteins collaborate to regulate the timing of Cyclin B protein expression in male meiotic prophase.Development (Cambridge, England) · 2023Article
- Chemi-Northern: a versatile chemiluminescent northern blot method for analysis and quantitation of RNA molecules.bioRxiv : the preprint server for biology · 2023Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Pumilio is an RNA-binding protein that represses a network of mRNAs to control embryogenesis, stem cell fate, fertility and neurological functions in Drosophila. We sought to identify the mechanism of Pumilio-mediated repression and find that it accelerates degradation of target mRNAs, mediated by three N-terminal Repression Domains (RDs), which are unique to Pumilio orthologs. We show that the repressive activities of the Pumilio RDs depend on specific subunits of the Ccr4-Not (CNOT) deadenylase complex. Depletion of Pop2, Not1, Not2, or Not3 subunits alleviates Pumilio RD-mediated repression of protein expression and mRNA decay, whereas depletion of other CNOT components had little or no effect. Moreover, the catalytic activity of Pop2 deadenylase is important for Pumilio RD activity. Further, we show that the Pumilio RDs directly bind to the CNOT complex. We also report that the decapping enzyme, Dcp2, participates in repression by the N-terminus of Pumilio. These results support a model wherein Pumilio utilizes CNOT deadenylase and decapping complexes to accelerate destruction of target mRNAs. Because the N-terminal RDs are conserved in mammalian Pumilio orthologs, the results of this work broadly enhance our understanding of Pumilio function and roles in diseases including cancer, neurodegeneration and epilepsy.
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