ArticleGenes & development2014
A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins.
Article in Genes & development, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
What it found
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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
58 citing papers in PubMed, 94 citations in OpenAlex.
- Polyadenylation of insulin mRNA by Tent5a regulates pancreatic beta cells.Nature communications · 2026Article
- A male-pheromone-elevated transcription factor ZNF362.1 in female schistosomes determines sexual maturation.Science advances · 2026Article
- Epigenetic Mechanisms Shaping Spine Regulation: Unveiling the Role of Cytoskeletal Dynamics and Localized Protein Synthesis.Molecular neurobiology · 2025Review
- Impact of Acute Endurance Exercise on Alternative Splicing in Skeletal Muscle.FASEB bioAdvances · 2025Article
- Transcriptome-wide association study of alternative polyadenylation identifies susceptibility genes in non-small cell lung cancer.Oncogene · 2025Article
- Differences in the soluble and insoluble proteome between primary tauopathies.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025Article
- Impact of Acute Endurance Exercise on Alternative Splicing in Skeletal Muscle.bioRxiv : the preprint server for biology · 2025Article
- Cytoplasmic regulation of the poly(A) tail length as a potential therapeutic target.RNA (New York, N.Y.) · 2025Review
- Article
- Inhibition ofeLife · 2024Article
- The Roles of Cytoplasmic Polyadenylation Element Binding Protein 1 in Tumorigenesis.Mini reviews in medicinal chemistry · 2024Review
- Cytoplasmic Polyadenylation Element Binding Protein 1 and Atherosclerosis: Prospective Target and New Insights.Current vascular pharmacology · 2024Review
- CPEB2 inhibit cell proliferation through upregulating p21 mRNA stability in glioma.Scientific reports · 2023Article
- Article
- Reviewing PTBP1 Domain Modularity in the Pre-Genomic Era: A Foundation to Guide the Next Generation of Exploring PTBP1 Structure-Function Relationships.International journal of molecular sciences · 2023Review
- CPEB2 Suppresses Hepatocellular Carcinoma Epithelial-Mesenchymal Transition and Metastasis through Regulating the HIF-1α/miR-210-3p/CPEB2 Axis.Pharmaceutics · 2023Article
- CPEB and translational control by cytoplasmic polyadenylation: impact on synaptic plasticity, learning, and memory.Molecular psychiatry · 2023Review
- Cytoplasmic Polyadenylation Is an Ancestral Hallmark of Early Development in Animals.Molecular biology and evolution · 2023Article
- FAM193A is a positive regulator of p53 activity.Cell reports · 2023Article
- Merits of Diazirine Photo-Immobilization for Target Profiling of Natural Products and Cofactors.ACS chemical biology · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytoplasmic changes in polyA tail length is a key mechanism of translational control and is implicated in germline development, synaptic plasticity, cellular proliferation, senescence, and cancer progression. The presence of a U-rich cytoplasmic polyadenylation element (CPE) in the 3' untranslated regions (UTRs) of the responding mRNAs gives them the selectivity to be regulated by the CPE-binding (CPEB) family of proteins, which recognizes RNA via the tandem RNA recognition motifs (RRMs). Here we report the solution structures of the tandem RRMs of two human paralogs (CPEB1 and CPEB4) in their free and RNA-bound states. The structures reveal an unprecedented arrangement of RRMs in the free state that undergo an original closure motion upon RNA binding that ensures high fidelity. Structural and functional characterization of the ZZ domain (zinc-binding domain) of CPEB1 suggests a role in both protein-protein and protein-RNA interactions. Together with functional studies, the structures reveal how RNA binding by CPEB proteins leads to an optimal positioning of the N-terminal and ZZ domains at the 3' UTR, which favors the nucleation of the functional ribonucleoprotein complexes for translation regulation.
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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.