Evidence map›Paper›PMID 26687677›Full record

ArticleMolecular cell2015

DGCR8 Acts as an Adaptor for the Exosome Complex to Degrade Double-Stranded Structured RNAs.

Sara Macias, Ross A Cordiner, Philippe Gautier, Mireya Plass, Javier F Cáceres

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed, 1 pooled it
4.2field-weighted citation impact, top 5% 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

56 citing papers in PubMed, 1 synthesis or guideline pooled it, 98 citations in OpenAlex.

  1. Pooled it
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  16. Embryonic microRNAs are essential for bovine preimplantation embryo development.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. An Insight into miR-1290: An Oncogenic miRNA with Diagnostic Potential.International journal of molecular sciences · 2022
    Review
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  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Sara MaciasMedical Research Council Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Edinburgh EH4 2XU, UK.
Ross A CordinerMedical Research Council Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Edinburgh EH4 2XU, UK.
Philippe GautierMedical Research Council Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Edinburgh EH4 2XU, UK.
Mireya PlassDepartment of Biology, Center for Computational and Applied Transcriptomics, University of Copenhagen, Ole Maaloes Vej 5, 2200 Copenhagen, Denmark.
Javier F CáceresMedical Research Council Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Edinburgh EH4 2XU, UK. Electronic address: javier.caceres@igmm.ed.ac.uk.
Medical Research Council · GBUniversity of Edinburgh · GBUniversity of Copenhagen · DK

Funding

Medical Research Council MC_PC_U127584479Wellcome Trust 095518Wellcome Trust 095518/Z/11/ZWellcome Trust 107665
6 · The paper itself

Abstract

The Microprocessor complex (DGCR8/Drosha) is required for microRNA (miRNA) biogenesis but also binds and regulates the stability of several types of cellular RNAs. Of particular interest, DGCR8 controls the stability of mature small nucleolar RNA (snoRNA) transcripts independently of Drosha, suggesting the existence of alternative DGCR8 complex(es) with other nucleases to process a variety of cellular RNAs. Here, we found that DGCR8 copurifies with subunits of the nuclear exosome, preferentially associating with its hRRP6-containing nucleolar form. Importantly, we demonstrate that DGCR8 is essential for the recruitment of the exosome to snoRNAs and to human telomerase RNA. In addition, we show that the DGCR8/exosome complex controls the stability of the human telomerase RNA component (hTR/TERC). Altogether, these data suggest that DGCR8 acts as an adaptor to recruit the exosome complex to structured RNAs and induce their degradation.

Indexed as

AnimalsEmbryonic Stem CellsExoribonucleasesExosome Multienzyme Ribonuclease ComplexExosomesHEK293 CellsHeLa CellsHumansMiceRNA-Binding ProteinsRNA, Double-StrandedRNA, Small NucleolarRNA StabilityRNA, TransferDGCR8 protein, humanExoribonucleasesEXOSC10 protein, humanExosome Multienzyme Ribonuclease ComplexRNA-Binding ProteinsRNA, Double-StrandedRNA, Small NucleolarRNA, Transfer

Identifiers

PMID26687677
PMCPMC4691244
OpenAlexW2192959916

What OpenQuestion holds

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Registered trials

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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.