Evidence map›Paper›PMID 27642082›Full record

ArticleNature communications2016

PRMT1-mediated methylation of MICU1 determines the UCP2/3 dependency of mitochondrial Ca(2+) uptake in immortalized cells.

Corina T Madreiter-Sokolowski, Christiane Klec, Warisara Parichatikanond, Sarah Stryeck, Benjamin Gottschalk, Sergio Pulido, Rene Rost, Emrah Eroglu, Nicole A Hofmann, Alexander I Bondarenko and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.5field-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

44 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
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  8. Targeting PRMT1 prevents acute and chronic graft-versus-host disease.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
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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

14 authors at 3 institutions in 2 countries.

Corina T Madreiter-SokolowskiCenter for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz, Harrachgasse 21/III, Graz 8010, Austria.
Christiane KlecCenter for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz, Harrachgasse 21/III, Graz 8010, Austria.
Warisara ParichatikanondCenter for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz, Harrachgasse 21/III, Graz 8010, Austria.
Sarah StryeckCenter for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz, Harrachgasse 21/III, Graz 8010, Austria.
Benjamin GottschalkCenter for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz, Harrachgasse 21/III, Graz 8010, Austria.
Sergio PulidoInstitute of Chemistry, University of Graz, Graz 8010, Austria.
Rene RostCenter for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz, Harrachgasse 21/III, Graz 8010, Austria.
Emrah ErogluCenter for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz, Harrachgasse 21/III, Graz 8010, Austria.ORCID http://orcid.org/0000-0002-9373-0808
Nicole A HofmannCenter for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz, Harrachgasse 21/III, Graz 8010, Austria.
Alexander I BondarenkoCenter for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz, Harrachgasse 21/III, Graz 8010, Austria.
Tobias MadlCenter for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz, Harrachgasse 21/III, Graz 8010, Austria.ORCID http://orcid.org/0000-0002-9725-5231
Markus Waldeck-WeiermairCenter for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz, Harrachgasse 21/III, Graz 8010, Austria.
Roland MalliCenter for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz, Harrachgasse 21/III, Graz 8010, Austria.
Wolfgang F GraierCenter for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz, Harrachgasse 21/III, Graz 8010, Austria.ORCID http://orcid.org/0000-0003-1871-3298
Medical University of Graz · ATCenter for Integrated Protein Science Munich · DEUniversity of Graz · AT

Funding

Austrian Science Fund FWF P 28529Austrian Science Fund FWF P 28854Austrian Science Fund FWF W 1226
6 · The paper itself

Abstract

Recent studies revealed that mitochondrial Ca(2+) channels, which control energy flow, cell signalling and death, are macromolecular complexes that basically consist of the pore-forming mitochondrial Ca(2+) uniporter (MCU) protein, the essential MCU regulator (EMRE), and the mitochondrial Ca(2+) uptake 1 (MICU1). MICU1 is a regulatory subunit that shields mitochondria from Ca(2+) overload. Before the identification of these core elements, the novel uncoupling proteins 2 and 3 (UCP2/3) have been shown to be fundamental for mitochondrial Ca(2+) uptake. Here we clarify the molecular mechanism that determines the UCP2/3 dependency of mitochondrial Ca(2+) uptake. Our data demonstrate that mitochondrial Ca(2+) uptake is controlled by protein arginine methyl transferase 1 (PRMT1) that asymmetrically methylates MICU1, resulting in decreased Ca(2+) sensitivity. UCP2/3 normalize Ca(2+) sensitivity of methylated MICU1 and, thus, re-establish mitochondrial Ca(2+) uptake activity. These data provide novel insights in the complex regulation of the mitochondrial Ca(2+) uniporter by PRMT1 and UCP2/3.

Indexed as

CalciumCalcium-Binding ProteinsCalcium ChannelsCation Transport ProteinsHeLa CellsHumansMethylationMitochondrial Membrane Transport ProteinsProtein-Arginine N-MethyltransferasesProtein Processing, Post-TranslationalRepressor ProteinsUncoupling Protein 2Uncoupling Protein 3CalciumCalcium-Binding ProteinsCalcium ChannelsCation Transport ProteinsMICU1 protein, humanmitochondrial calcium uniporterMitochondrial Membrane Transport ProteinsPRMT1 protein, humanProtein-Arginine N-MethyltransferasesRepressor ProteinsUCP2 protein, humanUCP3 protein, humanUncoupling Protein 2Uncoupling Protein 3

Identifiers

PMID27642082
PMCPMC5031806
OpenAlexW2521525326

What OpenQuestion holds

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LicenceCC BY
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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.