Evidence map›Paper›PMID 25776552›Full record

ArticleMolecular and cellular biology2015

Stomatin-like protein 2 is required for in vivo mitochondrial respiratory chain supercomplex formation and optimal cell function.

Panagiotis Mitsopoulos, Yu-Han Chang, Timothy Wai, Tim König, Stanley D Dunn, Thomas Langer, Joaquín Madrenas

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed, 1 pooled it
4.8field-weighted citation impact, top 4% 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

43 citing papers in PubMed, 1 synthesis or guideline pooled it, 99 citations in OpenAlex.

  1. Pooled it
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  15. Trophoblast Syncytialization: A Metabolic Crossroads.Results and problems in cell differentiation · 2024
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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

7 authors at 4 institutions in 2 countries.

Panagiotis MitsopoulosMicrobiome and Disease Tolerance Centre, Department of Microbiology and Immunology, McGill University, Montreal, Quebec, Canada.
Yu-Han ChangMicrobiome and Disease Tolerance Centre, Department of Microbiology and Immunology, McGill University, Montreal, Quebec, Canada.
Timothy WaiInstitute for Genetics, Cologne Excellence Cluster on Cellular Stress Responses in Aging Associated Diseases, Center for Molecular Medicine, University of Cologne, Cologne, Germany.
Tim KönigInstitute for Genetics, Cologne Excellence Cluster on Cellular Stress Responses in Aging Associated Diseases, Center for Molecular Medicine, University of Cologne, Cologne, Germany.
Stanley D DunnDepartment of Biochemistry, University of Western Ontario, London, Ontario, Canada.
Thomas LangerInstitute for Genetics, Cologne Excellence Cluster on Cellular Stress Responses in Aging Associated Diseases, Center for Molecular Medicine, University of Cologne, Cologne, Germany.
Joaquín MadrenasMicrobiome and Disease Tolerance Centre, Department of Microbiology and Immunology, McGill University, Montreal, Quebec, Canada joaquin.madrenas@mcgill.ca.
McGill University · CACologne Excellence Cluster on Cellular Stress Responses in Aging Associated Diseases · DEUniversity of Cologne · DEWestern University · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Stomatin-like protein 2 (SLP-2) is a mainly mitochondrial protein that is widely expressed and is highly conserved across evolution. We have previously shown that SLP-2 binds the mitochondrial lipid cardiolipin and interacts with prohibitin-1 and -2 to form specialized membrane microdomains in the mitochondrial inner membrane, which are associated with optimal mitochondrial respiration. To determine how SLP-2 functions, we performed bioenergetic analysis of primary T cells from T cell-selective Slp-2 knockout mice under conditions that forced energy production to come almost exclusively from oxidative phosphorylation. These cells had a phenotype characterized by increased uncoupled mitochondrial respiration and decreased mitochondrial membrane potential. Since formation of mitochondrial respiratory chain supercomplexes (RCS) may correlate with more efficient electron transfer during oxidative phosphorylation, we hypothesized that the defect in mitochondrial respiration in SLP-2-deficient T cells was due to deficient RCS formation. We found that in the absence of SLP-2, T cells had decreased levels and activities of complex I-III2 and I-III2-IV(1-3) RCS but no defects in assembly of individual respiratory complexes. Impaired RCS formation in SLP-2-deficient T cells correlated with significantly delayed T cell proliferation in response to activation under conditions of limiting glycolysis. Altogether, our findings identify SLP-2 as a key regulator of the formation of RCS in vivo and show that these supercomplexes are required for optimal cell function.

Indexed as

AnimalsCell ProliferationCells, CulturedElectron Transport Chain Complex ProteinsMembrane Potential, MitochondrialMembrane ProteinsMiceMice, KnockoutMitochondriaMitochondrial ProteinsNerve Tissue ProteinsOxidative PhosphorylationPhenotypeT-LymphocytesElectron Transport Chain Complex ProteinsMembrane ProteinsMitochondrial ProteinsNerve Tissue Proteinsstomatin-like protein 2, mouse

Identifiers

PMID25776552
PMCPMC4405640
OpenAlexW2166886529

What OpenQuestion holds

Textmetadata
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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.