Evidence map›Paper›PMID 31817188›Full record

ArticleViruses2019

The Cellular Localization of the p42 and p46 Oligoadenylate Synthetase 1 Isoforms and Their Impact on Mitochondrial Respiration.

Stig Skrivergaard, Monica Skou Jensen, Tine Breckling Rolander, Tram Bao Ngoc Nguyen, Amanda Bundgaard, Lene N Nejsum, Pia M Martensen

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

12 citing papers in PubMed, 15 citations in OpenAlex.

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  12. 2-5A-Mediated decay (2-5AMD): from antiviral defense to control of host RNA.Critical reviews in biochemistry and molecular biology
    Review
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

7 authors at 1 institution in 1 country.

Stig SkrivergaardDepartment Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark.
Monica Skou JensenDepartment Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark.
Tine Breckling RolanderDepartment Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark.
Tram Bao Ngoc NguyenDepartment Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark.
Amanda BundgaardDepartment Bioscience, Aarhus University, 8000 Aarhus C, Denmark.
Lene N NejsumDepartment Clinical Medicine, Aarhus University, 8200 Aarhus N, Denmark.
Pia M MartensenDepartment Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark.
Aarhus University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The importance of the IFN-induced oligoadenylate synthetase (OAS) proteins and the OAS/RNase L pathway in the innate response against viral pathogens is well-established, however the observed differences in anti-viral activity between the human OAS1 p46 and p42 isoforms are not fully understood. The protein expression of these isoforms is determined by the SNP rs10774671, either being an A or a G allele resulting in expression of either the p42 or the p46 isoform. Using fluorescence microscopy and immunoblot analysis of fractionated cell samples, we show here that the CaaX motif is of key importance to the cellular localization. The OAS1 p42 isoform is mainly located in the cytosol, whereas the p46 isoform with a C-terminal CaaX motif is translocated to membranous organelles, like the mitochondria. We furthermore observed differences between p42 and p46 in their effect on mitochondrial physiology using high resolution respirometry and fluorometry. Overexpression of OAS1 p42 and IFN-β treatment of HeLa cells (AA genotype) resulted in significantly increased respiration, which was not seen with p46 overexpression. The difference in subcellular localization and mitochondrial effect of these two OAS1 isoforms might help to explain the anti-viral mechanisms that differentiate these proteins.

Indexed as

Cell Respiration2',5'-Oligoadenylate SynthetaseHeLa CellsHumansInterferon-betaIntracellular SpaceMembrane Potential, MitochondrialMitochondriaOxygenProtein Transport2',5'-Oligoadenylate SynthetaseInterferon-betaOAS1 protein, humanOxygenCaaX motifcellular localizationhigh resolution respirometryISGmitochondrial transmembrane potentialOAS1oroborosoxygen consumption ratetype 1 inteferon

Identifiers

PMID31817188
PMCPMC6950736
OpenAlexW2993153513

What OpenQuestion holds

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LicenceCC BY
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.