ArticleCell reports2023
The human CNOT1-CNOT10-CNOT11 complex forms a structural platform for protein-protein interactions.
Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 23 citations in OpenAlex.
- Regulation of mRNA poly(A) tail length governs mammalian body plan formation in gastruloids.Nature communications · 2026Article
- CNOT10 is involved in the TTP-mediated AU-rich element-containing mRNA metabolism, independent of mRNA decay regulation.RNA (New York, N.Y.) · 2026Article
- Degron models: a toolbox for rapid in vivo depletion of essential proteins regulating mRNA metabolism.Communications biology · 2026Article
- CNOT11 depletion is associated with autophagy-related responses and IL-6-JAK-STAT signaling in cancer cells.Frontiers in cell and developmental biology · 2026Article
- Regulators of interferon-responsive microglia uncovered by Genome-wide CRISPRi screening.NPJ dementia · 2026Article
- Designing novel solenoid proteins with in silico evolution.Communications chemistry · 2025Article
- The CCR4-NOT complex: a multifaceted sensor of molecular signals instructing eukaryotic mRNA translation and stability.Nucleic acids research · 2025Review
- Article
- Exploring the CNOT1(800-999) HEAT Domain and Its Interactions with Tristetraprolin (TTP) as Revealed by Hydrogen/Deuterium Exchange Mass Spectrometry.Biomolecules · 2025Article
- The SP140-RESIST pathway regulates interferon mRNA stability and antiviral immunity.bioRxiv : the preprint server for biology · 2025Article
- The CCR4-NOT deadenylase complex mediates tubulin autoregulationmicroPublication biology · 2025Article
- GGNBP2 regulates MDA5 sensing triggered by self double-stranded RNA following loss of ADAR1 editing.Science immunology · 2024Article
- In Vitro Reconstitution of the Drosophila melanogaster CCR4-NOT Complex to Assay Deadenylation.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Reconstitution of Human CCR4-NOT Complex from Purified Proteins and an Assay of Its Deadenylation Activity.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Roles of the CCR4-Not complex in translation and dynamics of co-translation events.Wiley interdisciplinary reviews. RNA · 2023Review
- Specific recognition and ubiquitination of translating ribosomes by mammalian CCR4-NOT.Nature structural & molecular biology · 2023Article
- Structure and assembly of the NOT10:11 module of the CCR4-NOT complex.Communications biology · 2023Article
- Mechanism of ribosome-associated mRNA degradation during tubulin autoregulation.Molecular cell · 2023Article
- RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system.Nucleic acids research · 2023Article
- Regulation of eukaryotic mRNA deadenylation and degradation by the Ccr4-Not complex.Frontiers in cell and developmental biology · 2023Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The evolutionary conserved CCR4-NOT complex functions in the cytoplasm as the main mRNA deadenylase in both constitutive mRNA turnover and regulated mRNA decay pathways. The versatility of this complex is underpinned by its modular multi-subunit organization, with distinct structural modules actuating different functions. The structure and function of all modules are known, except for that of the N-terminal module. Using different structural approaches, we obtained high-resolution data revealing the architecture of the human N-terminal module composed of CNOT1, CNOT10, and CNOT11. The structure shows how two helical domains of CNOT1 sandwich CNOT10 and CNOT11, leaving the most conserved domain of CNOT11 protruding into solvent as an antenna. We discovered that GGNBP2, a protein identified as a tumor suppressor and spermatogenic factor, is a conserved interacting partner of the CNOT11 antenna domain. Structural and biochemical analyses thus pinpoint the N-terminal CNOT1-CNOT10-CNOT11 module as a conserved protein-protein interaction platform.
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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.