ArticleNucleic acids research2021
Crystal structure and functional properties of the human CCR4-CAF1 deadenylase complex.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 29 citations in OpenAlex.
- Global Regulatory Functions of the Human CCR4-NOT Complex in mRNA Deadenylation and Decay.bioRxiv : the preprint server for biology · 2026Article
- The SPN-4 Rbfox RNA-binding protein selects maternal mRNAs for CCR4-NOT-dependent clearance in early Caenorhabditis elegans embryos.Development (Cambridge, England) · 2026Article
- The CCR4-NOT complex: a multifaceted sensor of molecular signals instructing eukaryotic mRNA translation and stability.Nucleic acids research · 2025Review
- Discovery of Drug-like Inhibitors of the Human Caf1/CNOT7 poly(A)-Selective Nuclease Using Compound Screening.Biomolecules · 2025Article
- The E3 ubiquitin ligase, RNF219, suppresses CNOT6L expression to exhibit antiproliferative activity.FEBS open bio · 2025Article
- The SPN-4 Rbfox RNA-binding protein selects maternal mRNAs for CCR4-NOT-dependent clearance in earlybioRxiv : the preprint server for biology · 2025Article
- Characterization of nuclease stability and poly(A)-binding protein binding activity of chemically modified poly(A) tail forRSC chemical biology · 2025Article
- Resurgence of magnetic resonance techniques in the era of AlphaFold.Biophysical reviews · 2025Review
- Intracellular pathogen effector reprograms host gene expression by inhibiting mRNA decay.Nature communications · 2025Article
- Use of polyadenosine tail mimetics to enhance mRNA expression from genes associated with haploinsufficiency disorders.Molecular therapy. Nucleic acids · 2025Article
- Discovery of Substituted 5-(2-Hydroxybenzoyl)-2-Pyridone Analogues as Inhibitors of the Human Caf1/CNOT7 Ribonuclease.Molecules (Basel, Switzerland) · 2024Article
- Deadenylation kinetics of mixed poly(A) tails at single-nucleotide resolution.Nature structural & molecular biology · 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
- RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system.Nucleic acids research · 2023Article
- Article
- The human CNOT1-CNOT10-CNOT11 complex forms a structural platform for protein-protein interactions.Cell reports · 2023Article
- Regulation of eukaryotic mRNA deadenylation and degradation by the Ccr4-Not complex.Frontiers in cell and developmental biology · 2023Review
- Structure and function of molecular machines involved in deadenylation-dependent 5'-3' mRNA degradation.Frontiers in genetics · 2023Review
- Cytidine-containing tails robustly enhance and prolong protein production of synthetic mRNA in cell andMolecular therapy. Nucleic acids · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The CCR4 and CAF1 deadenylases physically interact to form the CCR4-CAF1 complex and function as the catalytic core of the larger CCR4-NOT complex. Together, they are responsible for the eventual removal of the 3'-poly(A) tail from essentially all cellular mRNAs and consequently play a central role in the posttranscriptional regulation of gene expression. The individual properties of CCR4 and CAF1, however, and their respective contributions in different organisms and cellular environments are incompletely understood. Here, we determined the crystal structure of a human CCR4-CAF1 complex and characterized its enzymatic and substrate recognition properties. The structure reveals specific molecular details affecting RNA binding and hydrolysis, and confirms the CCR4 nuclease domain to be tethered flexibly with a considerable distance between both enzyme active sites. CCR4 and CAF1 sense nucleotide identity on both sides of the 3'-terminal phosphate, efficiently differentiating between single and consecutive non-A residues. In comparison to CCR4, CAF1 emerges as a surprisingly tunable enzyme, highly sensitive to pH, magnesium and zinc ions, and possibly allowing distinct reaction geometries. Our results support a picture of CAF1 as a primordial deadenylase, which gets assisted by CCR4 for better efficiency and by the assembled NOT proteins for selective mRNA targeting and regulation.
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