Evidence map›Paper›PMID 25708700›Full record

ArticleCellular and molecular life sciences : CMLS2015

Mitochondrial fusion provides an 'initial metabolic complementation' controlled by mtDNA.

Liang Yang, Qi Long, Jinglei Liu, Haite Tang, Yuxing Li, Feixiang Bao, Dajiang Qin, Duanqing Pei, Xingguo Liu

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
3.0field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

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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

66 citing papers in PubMed, 89 citations in OpenAlex.

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

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

9 authors at 2 institutions in 1 country.

Liang YangKey Laboratory of Regenerative Biology, Guangdong Provincial Key Laboratory of Stem Cell and Regenerative Medicine, South China Institute for Stem Cell Biology and Regenerative Medicine, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China.
Qi Long
Jinglei Liu
Haite Tang
Yuxing Li
Feixiang Bao
Dajiang Qin
Duanqing Pei
Xingguo Liu
Chinese Academy of Sciences · CNGuangzhou Institutes of Biomedicine and Health · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heteroplasmic cells, harboring both mutant and normal mitochondrial DNAs (mtDNAs), must accumulate mutations to a threshold level before respiratory activity is affected. This phenomenon has led to the hypothesis of mtDNA complementation by inter-mitochondrial content mixing. The precise mechanisms of heteroplasmic complementation are unknown, but it depends both on the mtDNA nucleoid dynamics among mitochondria as well as the mitochondrial dynamics as influenced by mtDNA. We tracked nucleoids among the mitochondria in real time to show that they are shared after complete fusion but not 'kiss-and-run'. Employing a cell hybrid model, we further show that mtDNA-less mitochondria, which have little ATP production and extensive Opa1 proteolytic cleavage, exhibit weak fusion activity among themselves, yet remain competent in fusing with healthy mitochondria in a mitofusin- and OPA1-dependent manner, resulting in restoration of metabolic function. Depletion of mtDNA by overexpression of the matrix-targeted nuclease UL12.5 resulted in heterogeneous mitochondrial membrane potential (ΔΨm) at the organelle level in mitofusin-null cells but not in wild type. In this system, overexpression of mitofusins or application of the fusion-promoting drug M1 could partially rescue the metabolic damage caused by UL12.5. Interestingly, mtDNA transcription/translation is not required for normal mitochondria to restore metabolic function to mtDNA-less mitochondria by fusion. Thus, interplay between mtDNA and fusion capacity governs a novel 'initial metabolic complementation'.

Indexed as

Adenosine TriphosphateAnimalsBlotting, WesternCell FusionDNA, MitochondrialDNA PrimersFluorescent Antibody TechniqueGenetic VectorsGTP PhosphohydrolasesHeLa CellsHumansHybrid CellsMiceMicroscopy, ConfocalMitochondrial DynamicsMitochondrial Membrane Transport ProteinsAdenosine TriphosphateDNA, MitochondrialDNA PrimersGTP PhosphohydrolasesMfn1 protein, humanMitochondrial Membrane Transport Proteins

Identifiers

PMID25708700
PMCPMC11113443
OpenAlexW2025469330

What OpenQuestion holds

Textmetadata
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.