ArticleNature structural & molecular biology2016
Structure of the active form of Dcp1-Dcp2 decapping enzyme bound to m
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 65 citations in OpenAlex.
- Sequence-encoded autoinhibition couples mRNA decapping activity to phase separation.bioRxiv : the preprint server for biology · 2026Article
- RNA anchoring of Upf1 facilitates recruitment of Dcp2 in the NMD decapping complex.Nucleic acids research · 2025Article
- Fluorescence lifetime sorting reveals tunable enzyme interactions within cytoplasmic condensates.The Journal of cell biology · 2025Article
- Biochemical analysis of human eIF4E-DCP2 interaction: Implications for the relationship between translation initiation and decapping.PloS one · 2025Article
- Human DCP1 is crucial for mRNA decapping and possesses paralog-specific gene regulating functions.eLife · 2024Article
- LINE-1 mRNA 3' end dynamics shape its biology and retrotransposition potential.Nucleic acids research · 2024Article
- Eukaryotic mRNA decapping factors: molecular mechanisms and activity.The FEBS journal · 2023Review
- An actin remodeling role for Arabidopsis processing bodies revealed by their proximity interactome.The EMBO journal · 2023Article
- Quantitative reconstitution of yeast RNA processing bodies.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure and function of molecular machines involved in deadenylation-dependent 5'-3' mRNA degradation.Frontiers in genetics · 2023Review
- Photocaged 5' cap analogues for optical control of mRNA translation in cells.Nature chemistry · 2022Article
- Structural Insight into Molecular Inhibitory Mechanism of InsPJournal of virology · 2022Article
- Dcp2 C-terminaleLife · 2022Article
- Structure of the poxvirus decapping enzyme D9 reveals its mechanism of cap recognition and catalysis.Structure (London, England : 1993) · 2022Article
- Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022Review
- Discovery of cellular substrates of human RNA-decapping enzyme DCP2 using a stapled bicyclic peptide inhibitor.Cell chemical biology · 2021Article
- Review
- Mutations in genes encoding regulators of mRNA decapping and translation initiation: links to intellectual disability.Biochemical Society transactions · 2020Review
- A quantitative inventory of yeast P body proteins reveals principles of composition and specificity.eLife · 2020Article
- Pby1 is a direct partner of the Dcp2 decapping enzyme.Nucleic acids research · 2020Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Elimination of the 5' cap of eukaryotic mRNAs, known as decapping, is considered to be a crucial, irreversible and highly regulated step required for the rapid degradation of mRNA by Xrn1, the major cytoplasmic 5'-3' exonuclease. Decapping is accomplished by the recruitment of a protein complex formed by the Dcp2 catalytic subunit and its Dcp1 cofactor. However, this complex has a low intrinsic enzymatic activity and requires several accessory proteins such as the Lsm1-7 complex, Pat1, Edc1-Edc2 and/or Edc3 to be fully active. Here we present the crystal structure of the active form of the yeast Kluyveromyces lactis Dcp1-Dcp2 enzyme bound to its product (m
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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.