ArticleNucleic acids research2014
The activation of the decapping enzyme DCP2 by DCP1 occurs on the EDC4 scaffold and involves a conserved loop in DCP1.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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Who cites it
81 citing papers in PubMed, 123 citations in OpenAlex.
- N4BP1 uses tandem KH domains to associate with EDC4 and mRNA decapping factors in P-bodies.Communications biology · 2026Article
- RNA-binding proteins in the mouse lens: Functional classifications, expression profiling, and interaction studies of Carhsp1 with crystallin mRNAs.Developmental biology · 2026Article
- Bridging technical innovation and computational advances in studies of RNA-protein assemblies.Nature reviews. Genetics · 2026Review
- Global stabilization of the transcriptome in mitotic cells.The EMBO journal · 2026Article
- Conserved and divergent features of human mRNA decapping revealed by biochemical reconstitution.Nature communications · 2026Article
- The trypanosome mRNA decapping enzyme ALPH1 prefers caps without m7G methylation and produces diphosphate RNA.Nucleic acids research · 2026Article
- The Lsm1-7 complex couples 3'-end protection to histone H4 acetylation to maintain mRNA homeostasis in Fusarium graminearum.Nucleic acids research · 2026Article
- Hypoxia-mediated regulation of mRNA metabolism: from transcription to stability.Cell communication and signaling : CCS · 2025Review
- A protein-proximity screen reveals Ebola virus co-opts the mRNA decapping complex through the scaffold protein EDC4.Nature communications · 2025Article
- The molecular axis hnRNPU/circKCNK2/EDC4/IL-11 aggravates osteolytic bone metastasis of RCC.Oncogene · 2025Article
- Global inhibition of deadenylation stabilizes the transcriptome in mitotic cells.bioRxiv : the preprint server for biology · 2025Article
- EDC4 C-terminal domain scaffolds P-body assembly and links P-body dynamics to p53-mediated tumor suppression.RNA (New York, N.Y.) · 2025Article
- Cytoplasmic mRNA decay and quality control machineries in eukaryotes.Nature reviews. Genetics · 2025Review
- PLAA/UFD-3 regulates P-bodies through its intrinsic disordered domain.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Characterization of exoribonuclease XRN1 as a cancer target and identification of adenosine-3',5'-bisphosphate as a potent enzyme inhibitor.Communications biology · 2025Article
- The ribosome as a platform to coordinate mRNA decay.Nucleic acids research · 2025Review
- 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
- One RNA-binding protein, many decisions: integrating the transcript life cycle into neuronal regulation.Frontiers in molecular neuroscience · 2025Article
- Human DCP1 is crucial for mRNA decapping and possesses paralog-specific gene regulating functions.eLife · 2024Article
21 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The removal of the 5'-cap structure by the decapping enzyme DCP2 and its coactivator DCP1 shuts down translation and exposes the mRNA to 5'-to-3' exonucleolytic degradation by XRN1. Although yeast DCP1 and DCP2 directly interact, an additional factor, EDC4, promotes DCP1-DCP2 association in metazoan. Here, we elucidate how the human proteins interact to assemble an active decapping complex and how decapped mRNAs are handed over to XRN1. We show that EDC4 serves as a scaffold for complex assembly, providing binding sites for DCP1, DCP2 and XRN1. DCP2 and XRN1 bind simultaneously to the EDC4 C-terminal domain through short linear motifs (SLiMs). Additionally, DCP1 and DCP2 form direct but weak interactions that are facilitated by EDC4. Mutational and functional studies indicate that the docking of DCP1 and DCP2 on the EDC4 scaffold is a critical step for mRNA decapping in vivo. They also revealed a crucial role for a conserved asparagine-arginine containing loop (the NR-loop) in the DCP1 EVH1 domain in DCP2 activation. Our data indicate that DCP2 activation by DCP1 occurs preferentially on the EDC4 scaffold, which may serve to couple DCP2 activation by DCP1 with 5'-to-3' mRNA degradation by XRN1 in human cells.
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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.