ArticleNature communications2022
Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Mechanisms of transcription termination across the coding and noncoding loci of the genome.Nature reviews. Molecular cell biology · 2026Review
- DNTTIP2 coordinates RNA exosome activities to ensure fidelity of human ribosome assembly.Nature communications · 2026Article
- Spliceosomal proteins direct RNA methylation to modulate gene expression and silence retrotransposons.Nature communications · 2026Article
- Structural basis for the synergistic assembly of the snRNA export complex.Nature structural & molecular biology · 2025Article
- A nuclear RNA degradation code is recognized by PAXT for eukaryotic transcriptome surveillance.Molecular cell · 2025Article
- A bifunctional snoRNA with separable activities in guiding rRNA 2'-O-methylation and scaffolding gametogenesis effectors.Nature communications · 2025Article
- Finding new roles of classic biomolecular condensates in the nucleus: Lessons from fission yeast.Cell insight · 2024Review
- Nuclear mRNA decay: regulatory networks that control gene expression.Nature reviews. Genetics · 2024Review
- Mapping the dynamics of epigenetic adaptation in S. pombe during heterochromatin misregulation.Developmental cell · 2024Article
- RNA quality control factors nucleate Clr4/SUV39H and trigger constitutive heterochromatin assembly.Cell · 2024Article
- ELM-the Eukaryotic Linear Motif resource-2024 update.Nucleic acids research · 2024Article
- Dual agonistic and antagonistic roles of ZC3H18 provide for co-activation of distinct nuclear RNA decay pathways.Cell reports · 2023Article
- The molecular basis of heterochromatin assembly and epigenetic inheritance.Molecular cell · 2023Review
- Article
- Mechanistic insights into RNA surveillance by the canonical poly(A) polymerase Pla1 of the MTREC complex.Nature communications · 2023Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To eliminate specific or aberrant transcripts, eukaryotes use nuclear RNA-targeting complexes that deliver them to the exosome for degradation. S. pombe MTREC, and its human counterpart PAXT, are key players in this mechanism but inner workings of these complexes are not understood in sufficient detail. Here, we present an NMR structure of an MTREC scaffold protein Red1 helix-turn-helix domain bound to the Iss10 N-terminus and show this interaction is required for proper cellular growth and meiotic mRNA degradation. We also report a crystal structure of a Red1-Ars2 complex explaining mutually exclusive interactions of hARS2 with various ED/EGEI/L motif-possessing RNA regulators, including hZFC3H1 of PAXT, hFLASH or hNCBP3. Finally, we show that both Red1 and hZFC3H1 homo-dimerize via their coiled-coil regions indicating that MTREC and PAXT likely function as dimers. Our results, combining structures of three Red1 interfaces with in vivo studies, provide mechanistic insights into conserved features of MTREC/PAXT architecture.
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