ArticleRNA (New York, N.Y.)2016
The S. pombe mRNA decapping complex recruits cofactors and an Edc1-like activator through a single dynamic surface.
Article in RNA (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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
20 citing papers in PubMed, 29 citations in OpenAlex.
- Sequence-encoded autoinhibition couples mRNA decapping activity to phase separation.bioRxiv : the preprint server for biology · 2026Article
- Conserved and divergent features of human mRNA decapping revealed by biochemical reconstitution.Nature communications · 2026Article
- Gamete fusion triggers cytosolic functions and P-body recruitment of the RNA-binding protein Mei2 to drive fission yeast zygotic development.Genes & development · 2026Article
- Cytoplasmic mRNA decay and quality control machineries in eukaryotes.Nature reviews. Genetics · 2025Review
- Assessing the applicability ofJournal of biomolecular NMR · 2023Article
- Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022Review
- An overview of structural approaches to study therapeutic RNAs.Frontiers in molecular biosciences · 2022Review
- Biomolecular condensates amplify mRNA decapping by biasing enzyme conformation.Nature chemical biology · 2021Article
- Dcp2: an mRNA decapping enzyme that adopts many different shapes and forms.Current opinion in structural biology · 2019Review
- Pat1 activates late steps in mRNA decay by multiple mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- RNA degradomes reveal substrates and importance for dark and nitrogen stress responses of Arabidopsis XRN4.Nucleic acids research · 2019Article
- An updated gene atlas for maize reveals organ-specific and stress-induced genes.The Plant journal : for cell and molecular biology · 2019Article
- General decapping activators target different subsets of inefficiently translated mRNAs.eLife · 2018Article
- mRNA decapping: finding the right structures.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Control of mRNA decapping by autoinhibition.Nucleic acids research · 2018Article
- Structure of the activated Edc1-Dcp1-Dcp2-Edc3 mRNA decapping complex with substrate analog poised for catalysis.Nature communications · 2018Article
- Application of aRNA (New York, N.Y.) · 2018Article
- A synergistic network of interactions promotes the formation of in vitro processing bodies and protects mRNA against decapping.Nucleic acids research · 2017Article
- Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structure of the active form of Dcp1-Dcp2 decapping enzyme bound to mNature structural & molecular biology · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The removal of the 5' 7-methylguanosine mRNA cap structure (decapping) is a central step in the 5'-3' mRNA degradation pathway and is performed by the Dcp1:Dcp2 decapping complex. The activity of this complex is tightly regulated to prevent premature degradation of the transcript. Here, we establish that the aromatic groove of the EVH1 domain of Schizosaccharomyces pombe Dcp1 can interact with proline-rich sequences in the exonuclease Xrn1, the scaffolding protein Pat1, the helicase Dhh1, and the C-terminal disordered region of Dcp2. We show that this region of Dcp1 can also recruit a previously unidentified enhancer of decapping protein (Edc1) and solved the crystal structure of the complex. NMR relaxation dispersion experiments reveal that the Dcp1 binding site can adopt multiple conformations, thus providing the plasticity that is required to accommodate different ligands. We show that the activator Edc1 makes additional contacts with the regulatory domain of Dcp2 and that an activation motif in Edc1 increases the RNA affinity of Dcp1:Dcp2. Our data support a model where Edc1 stabilizes the RNA in the active site, which results in enhanced decapping rates. In summary, we show that multiple decapping factors, including the Dcp2 C-terminal region, compete with Edc1 for Dcp1 binding. Our data thus reveal a network of interactions that can fine-tune the catalytic activity of the decapping complex.
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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.