Evidence map›Paper›PMID 24848017›Full record

ArticleNucleic acids research2014

Global analysis of the nuclear processing of transcripts with unspliced U12-type introns by the exosome.

Elina H Niemelä, Ali Oghabian, Raymond H J Staals, Dario Greco, Ger J M Pruijn, Mikko J Frilander

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

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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

6 authors at 4 institutions in 2 countries.

Elina H NiemeläInstitute of Biotechnology, P.O. Box 56, FI-00014 University of Helsinki, Finland.
Ali OghabianInstitute of Biotechnology, P.O. Box 56, FI-00014 University of Helsinki, Finland.
Raymond H J StaalsDepartment of Biomolecular Chemistry, Radboud Institute for Molecular Life Sciences and Institute for Molecules and Materials, Radboud University Nijmegen,The Netherlands.
Dario GrecoUnit of Systems Toxicology, Finnish Institute of Occupational Health, Topeliuksenkatu 41 a A, FI-00250 Helsinki, Finland.
Ger J M PruijnDepartment of Biomolecular Chemistry, Radboud Institute for Molecular Life Sciences and Institute for Molecules and Materials, Radboud University Nijmegen,The Netherlands.
Mikko J FrilanderInstitute of Biotechnology, P.O. Box 56, FI-00014 University of Helsinki, Finland mikko.frilander@helsinki.fi.
Helsinki Institute of Physics · FIRadboud University Nijmegen · NLFinnish Institute of Occupational Health · FIUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

U12-type introns are a rare class of introns in the genomes of diverse eukaryotes. In the human genome, they number over 700. A subset of these introns has been shown to be spliced at a slower rate compared to the major U2-type introns. This suggests a rate-limiting regulatory function for the minor spliceosome in the processing of transcripts containing U12-type introns. However, both the generality of slower splicing and the subsequent fate of partially processed pre-mRNAs remained unknown. Here, we present a global analysis of the nuclear retention of transcripts containing U12-type introns and provide evidence for the nuclear decay of such transcripts in human cells. Using SOLiD RNA sequencing technology, we find that, in normal cells, U12-type introns are on average 2-fold more retained than the surrounding U2-type introns. Furthermore, we find that knockdown of RRP41 and DIS3 subunits of the exosome stabilizes an overlapping set of U12-type introns. RRP41 knockdown leads to slower decay kinetics of U12-type introns and globally upregulates the retention of U12-type, but not U2-type, introns. Our results indicate that U12-type introns are spliced less efficiently and are targeted by the exosome. These characteristics support their role in the regulation of cellular mRNA levels.

Indexed as

IntronsRNA Processing, Post-TranscriptionalRNA StabilityCell LineCell NucleusExosome Multienzyme Ribonuclease ComplexHumansRNA-Binding ProteinsRNA, MessengerRNA PrecursorsRNA, Small NuclearDIS3 protein, humanEXOSC4 protein, humanExosome Multienzyme Ribonuclease ComplexRNA-Binding ProteinsRNA, MessengerRNA PrecursorsRNA, Small NuclearU12 small nuclear RNA

Identifiers

PMID24848017
PMCPMC4066798
OpenAlexW2153491746

What OpenQuestion holds

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LicenceCC BY-NC
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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.