Evidence map›Paper›PMID 20531389›Full record

ArticleThe EMBO journal2010

Dis3-like 1: a novel exoribonuclease associated with the human exosome.

Raymond H J Staals, Alfred W Bronkhorst, Geurt Schilders, Shimyn Slomovic, Gadi Schuster, Albert J R Heck, Reinout Raijmakers, Ger J M Pruijn

Open access · bronzeAbstract read
In one paragraph

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 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
6.5field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

91 citing papers in PubMed, 145 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. International journal of molecular sciences · 2023
    Review
  16. Article
  17. Control of RNA degradation in cell fate decision.Frontiers in cell and developmental biology · 2023
    Review
  18. Article
  19. Article
  20. Article

31 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 5 institutions in 2 countries.

Raymond H J StaalsDepartment of Biomolecular Chemistry, Nijmegen Center for Molecular Life Sciences, Institute for Molecules and Materials, Radboud University Nijmegen, Nijmegen, The Netherlands.
Alfred W Bronkhorst
Geurt Schilders
Shimyn Slomovic
Gadi Schuster
Albert J R Heck
Reinout Raijmakers
Ger J M Pruijn
Radboud University Medical Center · NLTechnion – Israel Institute of Technology · ILUtrecht University · NLRadboud Institute for Molecular Life Sciences · NLRadboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The exosome is an exoribonuclease complex involved in the degradation and maturation of a wide variety of RNAs. The nine-subunit core of the eukaryotic exosome is catalytically inactive and may have an architectural function and mediate substrate binding. In Saccharomyces cerevisiae, the associated Dis3 and Rrp6 provide the exoribonucleolytic activity. The human exosome-associated Rrp6 counterpart contributes to its activity, whereas the human Dis3 protein is not detectably associated with the exosome. Here, a proteomic analysis of immunoaffinity-purified human exosome complexes identified a novel exosome-associated exoribonuclease, human Dis3-like exonuclease 1 (hDis3L1), which was confirmed to associate with the exosome core by co-immunoprecipitation. In contrast to the nuclear localization of Dis3, hDis3L1 exclusively localized to the cytoplasm. The hDis3L1 isolated from transfected cells degraded RNA in an exoribonucleolytic manner, and its RNB domain seemed to mediate this activity. The siRNA-mediated knockdown of hDis3L1 in HeLa cells resulted in elevated levels of poly(A)-tailed 28S rRNA degradation intermediates, indicating the involvement of hDis3L1 in cytoplasmic RNA decay. Taken together, these data indicate that hDis3L1 is a novel exosome-associated exoribonuclease in the cytoplasm of human cells.

Indexed as

Cell LineCytoplasmExoribonucleasesExosome Multienzyme Ribonuclease ComplexExosomesHumansMolecular Sequence DataProtein SubunitsRecombinant Fusion ProteinsRNASaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDIS3 protein, S cerevisiaeExoribonucleasesExosome Multienzyme Ribonuclease ComplexProtein SubunitsRecombinant Fusion ProteinsRNASaccharomyces cerevisiae Proteins

Identifiers

PMID20531389
PMCPMC2910272
OpenAlexW2025859016

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.