The 3' to 5' Exoribonuclease DIS3: From Structure and Mechanisms to Biological Functions and Role in Human Disease
Open accessAbstract
DIS3 is a conserved exoribonuclease and catalytic subunit of the exosome, a protein complex involved in the 3' to 5' degradation and processing of both nuclear and cytoplasmic RNA species. Recently, aberrant expression of DIS3 has been found to be implicated in a range of different cancers. Perhaps most striking is the finding that DIS3 is recurrently mutated in 11% of multiple myeloma patients. Much work has been done to elucidate the structural and biochemical characteristics of DIS3, including the mechanistic details of its role as an effector of RNA decay pathways. Nevertheless, we do not understand how DIS3 mutations can lead to cancer. There are a number of studies that pertain to the function of DIS3 at the organismal level. Mutant phenotypes in S. pombe, S. cerevisiae and Drosophila suggest DIS3 homologues have a common role in cell-cycle progression and microtubule assembly. DIS3 has also recently been implicated in antibody diversification of mouse B-cells. This article aims to review current knowledge of the structure, mechanisms and functions of DIS3 as well as highlighting the genetic patterns observed within myeloma patients, in order to yield insight into the putative role of DIS3 mutations in oncogenesis.
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Association of DIS3 and EXOSC10 with the RNA exosome decreases catalytic efficiency through allosteric effects.
“It has also been suggested that association of DIS3 and EXOSC10 with the RNA exosome decreases catalytic efficiency through allosteric effects42,69.”
From EXOSC3 G191 Variants Trigger System-Wide Recalibration of RNA Processing Machinery (2026) · cites this paper as [69]
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“It has also been suggested that association of DIS3 and EXOSC10 with the RNA exosome decreases catalytic efficiency through allosteric effects 42,69 .”
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Human DDX6 regulates translation and decay of inefficiently translated mRNAsPreprint
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Human DDX6 regulates translation and decay of inefficiently translated mRNAsPreprint
Weber, R., Wohlbold, L., & Chang, C.-T. (2024) · eLife · doi:10.7554/elife.92426.2
Weber, R., Wohlbold, L., & Chang, C.-T. (2024) · eLife · doi:10.7554/elife.92426.2.sa0
Author response: Human DDX6 regulates translation and decay of inefficiently translated mRNAs
Weber, R., Wohlbold, L., & Chang, C.-T. (2024) · eLife · doi:10.7554/elife.92426.2.sa3
eLife Assessment: Human DDX6 regulates translation and decay of inefficiently translated mRNAs
VijayRaghavan, K. (2024) · eLife · doi:10.7554/elife.92426.2.sa2
Weber, R., Wohlbold, L., & Chang, C.-T. (2024) · eLife · doi:10.7554/elife.92426.2.sa1
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- Authors
- Robinson, S., Oliver, A., Chevassut, T., & Newbury, S.
- Affiliations
- Brighton and Sussex Medical School (GB)
- University of Sussex (GB)
- Corresponding author
- Newbury, Sarah
- Venue
- Biomolecules
- Publisher
- MDPI AG
- Published
- 2015-07-17
- Volume
- 5
- Issue
- 3
- Pages
- 1515-1539
- ISSN
- 2218-273X (ISSN-L)
- PMC
- PMC4598762
- OpenAlex
- W1784611664
- Cited by
- 71
- References
- 116
- Citations by year
- 2026: 7 · 2025: 1 · 2024: 16 · 2023: 8 · 2022: 4 · 2021: 8 · 2020: 4 · 2019: 10 · 2018: 3 · 2017: 5 · 2016: 4 · 2015: 1
- FWCI
- 0.42
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- Biomolecules (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Sussex Research Online (University of Sussex) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- Brighton and Sussex Medical School (WC-003-14)
- BBSRC (BB/I021345/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- DIS3, exoribonuclease, exosomes, RNA degradation, multiple myeloma, carcinogenesis, cell cycle progression, microtubule assembly, antibody diversification, B cells, Schizosaccharomyces pombe, Saccharomyces cerevisiae, Drosophila
- MeSH terms
- Animals, Disease, Humans, Conserved Sequence, Protein Transport, Exosome Multienzyme Ribonuclease Complex
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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