ArticleRNA (New York, N.Y.)2011
Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition.
Article in RNA (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed, 51 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
- Eukaryotic mRNA decapping factors: molecular mechanisms and activity.The FEBS journal · 2023Review
- Article
- Decapping factor Dcp2 controls mRNA abundance and translation to adjust metabolism and filamentation to nutrient availability.bioRxiv : the preprint server for biology · 2023Article
- Dcp2 C-terminaleLife · 2022Article
- Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022Review
- Dcp2: an mRNA decapping enzyme that adopts many different shapes and forms.Current opinion in structural biology · 2019Review
- General decapping activators target different subsets of inefficiently translated mRNAs.eLife · 2018Article
- Structural and molecular mechanisms for the control of eukaryotic 5'-3' mRNA decay.Nature structural & molecular biology · 2018Review
- 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 unique surface on Pat1 C-terminal domain directly interacts with Dcp2 decapping enzyme and Xrn1 5'-3' mRNA exonuclease in yeast.Proceedings of the National Academy of Sciences of the United States of America · 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
- 5' to 3' mRNA Decay Contributes to the Regulation of Arabidopsis Seed Germination by Dormancy.Plant physiology · 2017Article
- New insights into decapping enzymes and selective mRNA decay.Wiley interdisciplinary reviews. RNA · 2017Review
- Structure of the active form of Dcp1-Dcp2 decapping enzyme bound to mNature structural & molecular biology · 2016Article
- Structural basis of mRNA-cap recognition by Dcp1-Dcp2.Nature structural & molecular biology · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Cap hydrolysis is a critical step in several eukaryotic mRNA decay pathways and is carried out by the evolutionarily conserved decapping complex containing Dcp2 at the catalytic core. In yeast, Dcp1 is an essential activator of decapping and coactivators such as Edc1 and Edc2 are thought to enhance activity, though their mechanism remains elusive. Using kinetic analysis we show that a crucial function of Dcp1 is to couple the binding of coactivators of decapping to activation of Dcp2. Edc1 and Edc2 bind Dcp1 via its EVH1 proline recognition site and stimulate decapping by 1000-fold, affecting both the K(M) for mRNA and rate of the catalytic step. The C-terminus of Edc1 is necessary and sufficient to enhance the catalytic step, while the remainder of the protein likely increases mRNA binding to the decapping complex. Lesions in the Dcp1 EVH1 domain or the Edc1 proline-rich sequence are sufficient to block stimulation. These results identify a new role of Dcp1, which is to link the binding of coactivators to substrate recognition and activation of Dcp2.
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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.