ArticleMolecular and cellular biology2008
Similar modes of interaction enable Trailer Hitch and EDC3 to associate with DCP1 and Me31B in distinct protein complexes.
Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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71 citing papers in PubMed, 102 citations in OpenAlex.
- Bruno 1 remodels P-bodies to protect select mRNAs during the early ER stress response.Life science alliance · 2026Article
- Deadenylation and decapping factors cooperatively stimulate biochemical activities of DEAD-box ATPase Dhh1.Nucleic acids research · 2026Article
- Deadenylation and Decapping Factors Cooperatively Stimulate Biochemical Activities of DEAD-Box ATPase Dhh1.bioRxiv : the preprint server for biology · 2026Article
- ATF4-dependent upregulation of Bruno 1 remodels P-bodies to selectively protect mRNAs during ER stress throughoutbioRxiv : the preprint server for biology · 2026Article
- Bioinformatic Analyses of the Ataxin-2 Family Since Algae Emphasize Its Small Isoforms, Large Chimerisms, and the Importance of Human Exon 1B as Target of Therapies to Prevent Neurodegeneration.International journal of molecular sciences · 2026Article
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- Decapping activators Edc3 and Scd6 act redundantly with Dhh1 in post-transcriptional repression of starvation-induced pathways.bioRxiv : the preprint server for biology · 2025Article
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- Musashi-dependent mRNA translational activation is mediated through association with the Scd6/Like-sm family member, LSM14B.Scientific reports · 2025Article
- The role of ER exit sites in maintaining P-body organization and integrity during Drosophila melanogaster oogenesis.EMBO reports · 2025Article
- The mRNA dynamics underpinning translational control mechanisms of Drosophila melanogaster oogenesis.Biochemical Society transactions · 2024Review
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- The role of ER exit sites in maintaining P-body organization and transmitting ER stress response duringbioRxiv : the preprint server for biology · 2024Article
- Muskelin acts as a substrate receptor of the highly regulatedbioRxiv : the preprint server for biology · 2024Article
- Greatwall-Endos-PP2A/B55Open biology · 2024Article
- Me31B: a key repressor in germline regulation and beyond.Bioscience reports · 2024Review
- Eukaryotic mRNA decapping factors: molecular mechanisms and activity.The FEBS journal · 2023Review
- Review
- Mutational analysis of the functional motifs of the DEAD-box RNA helicase Me31B/DDX6 in Drosophila germline development.FEBS letters · 2023Article
- RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system.Nucleic acids research · 2023Article
11 more citing papers are in PubMed but not listed here.
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8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Trailer Hitch (Tral or LSm15) and enhancer of decapping-3 (EDC3 or LSm16) are conserved eukaryotic members of the (L)Sm (Sm and Like-Sm) protein family. They have a similar domain organization, characterized by an N-terminal LSm domain and a central FDF motif; however, in Tral, the FDF motif is flanked by regions rich in charged residues, whereas in EDC3 the FDF motif is followed by a YjeF_N domain. We show that in Drosophila cells, Tral and EDC3 specifically interact with the decapping activator DCP1 and the DEAD-box helicase Me31B. Nevertheless, only Tral associates with the translational repressor CUP, whereas EDC3 associates with the decapping enzyme DCP2. Like EDC3, Tral interacts with DCP1 and localizes to mRNA processing bodies (P bodies) via the LSm domain. This domain remains monomeric in solution and adopts a divergent Sm fold that lacks the characteristic N-terminal alpha-helix, as determined by nuclear magnetic resonance analyses. Mutational analysis revealed that the structural integrity of the LSm domain is required for Tral both to interact with DCP1 and CUP and to localize to P-bodies. Furthermore, both Tral and EDC3 interact with the C-terminal RecA-like domain of Me31B through their FDF motifs. Together with previous studies, our results show that Tral and EDC3 are structurally related and use a similar mode to associate with common partners in distinct protein complexes.
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