ArticleThe EMBO journal2010
The human core exosome interacts with differentially localized processive RNases: hDIS3 and hDIS3L.
Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 174 papers.
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Who cites it
174 citing papers in PubMed.
- Review
- RAN Translation-Coupled Decay of theInternational journal of molecular sciences · 2026Article
- Precision in RNA degradation: helicases, ribosome and RNA polymerase stalling, and RNA modifications.Trends in cell biology · 2026Review
- Cellular assembly and functional resilience of the mammalian RNA exosome.The EMBO journal · 2026Article
- Review
- Genetic and genomic approaches to explore roles for the conserved 3'-5' exoribonuclease EXOSC10 in normal and malignant cells.RNA (New York, N.Y.) · 2026Review
- ADAR1 and ADAR2 associate with the RNA exosome and modulate RNA stability.Nucleic acids research · 2026Article
- DIS3 mutations enhance AID-driven translocations during B-cell activation, promoting transformation to multiple myeloma.Nature communications · 2026Article
- HELZ2 RegulatesCirculation · 2026Article
- Widespread mono- and oligoadenylation direct small noncoding RNA maturation versus degradation fates.The EMBO journal · 2026Article
- Nuclear effects play an important role in determining codon usage-dependent human gene expression.Nature communications · 2025Article
- Defining the roles of the Integrator, NEXT, and nuclear exosome complexes in Drosophila oogenesis.Cell reports · 2025Article
- Identification of human pathways acting on nuclear non-coding RNAs using the Mirror forward genetic approach.Nature communications · 2025Article
- DIS3L, cytoplasmic exosome catalytic subunit, is essential for development but not cell viability in mice.RNA (New York, N.Y.) · 2025Article
- The CCR4-NOT deadenylase complex mediates tubulin autoregulationmicroPublication biology · 2025Article
- RNA 3'end tailing safeguards cells against products of pervasive transcription termination.Nature communications · 2024Article
- Article
- A Comparative Overview of the Role of Human Ribonucleases in Nonsense-Mediated mRNA Decay.Genes · 2024Article
- A UTP3-dependent nucleolar translocation pathway facilitates pre-rRNA 5'ETS processing.Nucleic acids research · 2024Article
- MYC Induces Oncogenic Stress through RNA Decay and Ribonucleotide Catabolism in Breast Cancer.Cancer discovery · 2024Article
114 more citing papers are in PubMed but not listed here.
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12 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The eukaryotic RNA exosome is a ribonucleolytic complex involved in RNA processing and turnover. It consists of a nine-subunit catalytically inert core that serves a structural function and participates in substrate recognition. Best defined in Saccharomyces cerevisiae, enzymatic activity comes from the associated subunits Dis3p (Rrp44p) and Rrp6p. The former is a nuclear and cytoplasmic RNase II/R-like enzyme, which possesses both processive exo- and endonuclease activities, whereas the latter is a distributive RNase D-like nuclear exonuclease. Although the exosome core is highly conserved, identity and arrangements of its catalytic subunits in different vertebrates remain elusive. Here, we demonstrate the association of two different Dis3p homologs--hDIS3 and hDIS3L--with the human exosome core. Interestingly, these factors display markedly different intracellular localizations: hDIS3 is mainly nuclear, whereas hDIS3L is strictly cytoplasmic. This compartmental distribution reflects the substrate preferences of the complex in vivo. Both hDIS3 and hDIS3L are active exonucleases; however, only hDIS3 has retained endonucleolytic activity. Our data suggest that three different ribonucleases can serve as catalytic subunits for the exosome in human cells.
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