Evidence map›Paper›PMID 17351641›Full record

ArticleNature cell biology2007

Uncoupling proteins 2 and 3 are fundamental for mitochondrial Ca2+ uniport.

Michael Trenker, Roland Malli, Ismene Fertschai, Sanja Levak-Frank, Wolfgang F Graier

Erratum issuedAbstract read
In one paragraph

Article in Nature cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 166 papers.

0numbers the graph read from it
0cells of the map it votes in
166citing papers in PubMed
–field-weighted citation impact
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

166 citing papers in PubMed.

  1. Trial
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  11. Article
  12. Article
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  14. Mitochondrial Calcium: Effects of Its Imbalance in Disease.Antioxidants (Basel, Switzerland) · 2022
    Review
  15. Article
  16. Review
  17. Mitochondrial CaInternational journal of molecular sciences · 2022
    Review
  18. Review
  19. Review
  20. Uncoupling Proteins and Regulated Proton Leak in Mitochondria.International journal of molecular sciences · 2022
    Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Michael Trenker *Institute of Molecular Biology and Biochemistry, Centre of Molecular Medicine, Medical University of Graz, Harrachgasse 21/III, 8010 Graz, Austria.
Roland Malli *Institute of Molecular Biology and Biochemistry, Centre of Molecular Medicine, Medical University of Graz, Harrachgasse 21/III, 8010 Graz, Austria.
Ismene FertschaiInstitute of Molecular Biology and Biochemistry, Centre of Molecular Medicine, Medical University of Graz, Harrachgasse 21/III, 8010 Graz, Austria.
Sanja Levak-FrankInstitute of Molecular Biology and Biochemistry, Centre of Molecular Medicine, Medical University of Graz, Harrachgasse 21/III, 8010 Graz, Austria.
Wolfgang F Graier *Institute of Molecular Biology and Biochemistry, Centre of Molecular Medicine, Medical University of Graz, Harrachgasse 21/III, 8010 Graz, Austria.

Funding

Austrian Science Fund FWF F 3010Austrian Science Fund FWF P 16860
6 · The paper itself

Abstract

Mitochondrial Ca(2+) uptake is crucial for the regulation of the rate of oxidative phosphorylation, the modulation of spatio-temporal cytosolic Ca(2+) signals and apoptosis. Although the phenomenon of mitochondrial Ca(2+) sequestration, its characteristics and physiological consequences have been convincingly reported, the actual protein(s) involved in this process are unknown. Here, we show that the uncoupling proteins 2 and 3 (UCP2 and UCP3) are essential for mitochondrial Ca(2+) uptake. Using overexpression, knockdown (small interfering RNA) and mutagenesis experiments, we demonstrate that UCP2 and UCP3 are elementary for mitochondrial Ca(2+) sequestration in response to cell stimulation under physiological conditions - observations supported by isolated liver mitochondria of Ucp2(-/-) mice lacking ruthenium red-sensitive Ca(2+) uptake. Our results reveal a novel molecular function for UCP2 and UCP3, and may provide the molecular mechanism for their reported effects. Moreover, the identification of proteins fundemental for mitochondrial Ca(2+) uptake expands our knowledge of the physiological role for mitochondrial Ca(2+) sequestration.

Indexed as

Amino Acid SequenceAnimalsCalciumCell LineCHO CellsCricetinaeCricetulusHeLa CellsHumansImmunoblottingIon ChannelsMiceMicroscopy, ConfocalMitochondriaMitochondria, LiverMitochondrial ProteinsCalciumIon ChannelsMitochondrial ProteinsRNA, Small InterferingUCP2 protein, humanUcp2 protein, mouseUCP3 protein, humanUcp3 protein, mouseUncoupling Protein 2Uncoupling Protein 3

Identifiers

PMID17351641
PMCPMC4060164

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.