ArticleThe EMBO journal2002
Identification of a ubiquitin-protein ligase subunit within the CCR4-NOT transcription repressor complex.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 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.
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.
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Who cites it
109 citing papers in PubMed, 215 citations in OpenAlex.
- High-throughput mapping of modular regulatory domains in human RNA-binding proteins.Cell systems · 2026Article
- Human CCR4-NOT suppresses pervasive transcription and retrotransposable elements.bioRxiv : the preprint server for biology · 2026Article
- Multi-omics analysis reveals the effects of prenatal nutrition on carcass-related tissues in beef cattle.Scientific reports · 2025Article
- The CCR4-NOT complex: a multifaceted sensor of molecular signals instructing eukaryotic mRNA translation and stability.Nucleic acids research · 2025Review
- Bioinformatics analysis identifies Mot2 protein as a potential regulator of autophagy inmicroPublication biology · 2025Article
- Targeted protein degradation using chimeric human E2 ubiquitin-conjugating enzymes.Communications biology · 2024Article
- PRC1 Protein Subcomplexes Architecture: Focus on the Interplay between Distinct PCGF Subunits in Protein Interaction Networks.International journal of molecular sciences · 2024Article
- The role of ubiquitin-conjugating enzyme in the process of spermatogenesis.Reproductive biology and endocrinology : RB&E · 2024Review
- Genome and GWAS analysis identified genes significantly related to phenotypic state ofHorticulture research · 2024Article
- Nedd4-2-dependent regulation of astrocytic Kir4.1 and Connexin43 controls neuronal network activity.The Journal of cell biology · 2024Article
- Specific recognition and ubiquitination of translating ribosomes by mammalian CCR4-NOT.Nature structural & molecular biology · 2023Article
- Disruption of the Mammalian Ccr4-Not Complex Contributes to Transcription-Mediated Genome Instability.Cells · 2023Article
- Conservation and Expansion of Transcriptional Factor Repertoire in theJournal of fungi (Basel, Switzerland) · 2023Article
- Conservation and Expansion of Transcriptional Factor Repertoire in thebioRxiv : the preprint server for biology · 2023Article
- Delineation of the clinical profile of CNOT2 haploinsufficiency and overview of the IDNADFS phenotype.Clinical genetics · 2023Article
- The RAG1 Ubiquitin Ligase Domain Stimulates Recombination of TCRβ and TCRα Genes and Influences Development of αβ T Cell Lineages.Journal of immunology (Baltimore, Md. : 1950) · 2022Article
- The CNOT4 Subunit of the CCR4-NOT Complex is Involved in mRNA Degradation, Efficient DNA Damage Repair, and XY Chromosome Crossover during Male Germ Cell Meiosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- The Arabidopsis NOT4A E3 ligase promotes PGR3 expression and regulates chloroplast translation.Nature communications · 2021Article
- CNOT4 enhances the efficacy of anti-PD-1 immunotherapy in a model of non-small cell lung cancer.FEBS open bio · 2020Article
- Review
49 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RING finger protein CNOT4 is a component of the CCR4-NOT complex. This complex is implicated in repression of RNA polymerase II transcription. Here we demonstrate that CNOT4 functions as a ubiquitin-protein ligase (E3). We show that the unique C4C4 RING domain of CNOT4 interacts with a subset of ubiquitin-conjugating enzymes (E2s). Using NMR spectroscopy, we detail the interaction of CNOT4 with UbcH5B and characterize RING residues that are critical for this interaction. CNOT4 acts as a potent E3 ligase in vitro. Mutations that destabilize the E2-E3 interface abolish this activity. Based on these results, we present a model of how E3 ligase function within the CCR4-NOT complex relates to transcriptional regulation.
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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.