Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations
Open accessAbstract
Mitochondria are highly mobile and dynamic organelles that continually fuse and divide. These processes allow mitochondria to exchange contents, including mitochondrial DNA (mtDNA). Here we examine the functions of mitochondrial fusion in differentiated skeletal muscle through conditional deletion of the mitofusins Mfn1 and Mfn2, mitochondrial GTPases essential for fusion. Loss of the mitofusins causes severe mitochondrial dysfunction, compensatory mitochondrial proliferation, and muscle atrophy. Mutant mice have severe mtDNA depletion in muscle that precedes physiological abnormalities. Moreover, the mitochondrial genomes of the mutant muscle rapidly accumulate point mutations and deletions. In a related experiment, we find that disruption of mitochondrial fusion strongly increases mitochondrial dysfunction and lethality in a mouse model with high levels of mtDNA mutations. With its dual function in safeguarding mtDNA integrity and preserving mtDNA function in the face of mutations, mitochondrial fusion is likely to be a protective factor in human disorders associated with mtDNA mutations.
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The muscle-specific deletion of Mfn1/Mfn2 genes was performed using the same driver as conditional OPA1 ablation, but only some phenotypes appear to be in common.
“Importantly, the muscle-specific deletion of Mfn1/Mfn2 genes was performed by using the same driver that we used here for conditional OPA1 ablation, but only some phenotypes appear to be in common.”
From Age-Associated Loss of OPA1 in Muscle Impacts Muscle Mass, Metabolic Homeostasis, Systemic Inflammation, and Epithelial Senescence (2017) · cites this paper as Chen et al., 2010
A reduced muscle mass has been reported in mice ablated for both Mfn1 and Mfn2.
“A reduced muscle mass has been also reported in mice ablated for both Mfn1 and Mfn2, although analyses of muscle stem cell and of protein synthesis were not shown (Chen et al., 2010).”
From Age-Associated Loss of OPA1 in Muscle Impacts Muscle Mass, Metabolic Homeostasis, Systemic Inflammation, and Epithelial Senescence (2017) · cites this paper as Chen et al., 2010
Mitochondrial fission is a quality control mechanism that isolates damaged or dysfunctional mitochondrial segments for removal by mitophagy.
“Furthermore, mitochondrial fission is another important quality control mechanism, isolating damaged or dysfunctional mitochondrial segments for removal by mitophagy [45].”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [45]
Cells engineered to contain a mix of wild-type and pathogenic mitochondria remain functional until the proportion of pathogenic mitochondria surpasses a critical threshold.
“Notably, cells engineered to contain a mix of wild-type and pathogenic mitochondria remain functional until the proportion of pathogenic mitochondria surpasses a critical threshold [45].”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [45]
Mitochondrial fusion prior to reaching the critical threshold stabilizes mtDNA copy number and prevents accumulation of mtDNA mutations.
“This protective mechanism of mitochondrial fusion, prior to reaching the critical threshold, primarily operates through stabilizing mtDNA copy number and preventing the accumulation of mtDNA mutations [45].”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [45]
Conditional deletion of Mfn1 and Mfn2 results in severe mtDNA depletion in muscle and causes severe mitochondrial dysfunction, compensatory mitochondrial proliferation, and muscle atrophy.
“Indeed, conditional deletion of Mfn1 and Mfn2 results in severe mtDNA depletion in muscle and causes severe mitochondrial dysfunction, compensatory mitochondrial proliferation, and muscle atrophy [45].”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [45]
Muscle-specific simultaneous ablation of MFN1 and MFN2 induces profound muscle atrophy.
“Muscle-specific simultaneous ablation of MFN1 and MFN2 induces profound muscle atrophy.”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [190]
Knockout mice with muscle-specific simultaneous ablation of MFN1 and MFN2 are viable at birth but display muscle growth defects characterized by mitochondrial dysfunction, reduction of mtDNA in skeletal muscle, and accumulation of point mutations and deletions in the mitochondrial genome that cause death within 6-8 weeks of age.
“Knockout mice are viable at birth, but they display muscle growth defects characterized by mitochondrial dysfunction, reduction of mitochondrial DNA (mtDNA) in skeletal muscle, and accumulation of point mutations deletions in the mitochondrial genome that cause death within 6–8 weeks of age [190].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [190]
Muscle-specific ablation of both Mfn1 and Mfn2 induces muscle atrophy and abnormal muscle growth in mice.
“Muscle-specific ablation of both Mfn1 and Mfn2 induces muscle atrophy and abnormal muscle growth in mice [4].”
From Inhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles (2019) · cites this paper as [4]
Failure in mitochondrial-shaping processes has detrimental consequences for the maintenance of muscle mass and function.
“Accordingly, the failure in mitochondrial-shaping processes has detrimental consequences for the maintenance of muscle mass and function [4,5,6,7,8,13,29].”
From Inhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles (2019) · cites this paper as [4]
Mitochondrial fusion proteins are essential for the maintenance of mitochondrial and skeletal muscle health.
“Taken altogether, the available literature clearly indicates that mitochondrial fusion proteins are essential for the maintenance of mitochondrial and skeletal muscle health.”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [33]
Mice lacking both Mfn-1 and Mfn-2 in skeletal muscle display severe mitochondrial dysfunction, accumulation of mitochondrial DNA damage, and a severe deficit in growth.
“It was, for instance, reported that mice lacking both Mfn-1 and Mfn-2 in skeletal muscle display severe mitochondrial dysfunction, accumulation of mitochondrial DNA damage, and a severe deficit in growth [33].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [33]
Muscle-specific deletion of Mfn1 and Mfn2 results in accumulation of mtDNA mutations and deletions, reduced mtDNA content, and muscle atrophy.
“Muscle-specific deletion of Mfn1 and Mfn2 results in the accumulation of mtDNA mutations and deletions, reduced mtDNA content, as well as muscle atrophy.(Chen, Vermulst, Wang, Chomyn, Prolla, McCaffery, and Chan 2010)”
From Successful aging: Advancing the science of physical independence in older adults (2015) · cites this paper as Chen et al. 2010
Genetic loss of function of Mfn2 and Opa1 in mice is sufficient to cause sarcopenia.
“Interestingly, genetic loss of function of Mfn2 and Opa1 in mice is sufficient to cause sarcopenia43–45”
From Mitochondrial oxidative capacity and NAD+ biosynthesis are reduced in human sarcopenia across ethnicities (2019) · cites this paper as [43]
The quality of mitochondria has emerged as an important control process that regulates skeletal muscle function.
“Recently, the quality of mitochondria has emerged as important control process that regulates skeletal muscle function20–23.”
From Disuse-associated loss of the protease Lonp1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass and strength (2022) · cites this paper as [20]
Proper maintenance of mitochondria dynamics, i.e. the balance between fission and fusion, is necessary for optimal muscle mitochondrial function and fitness.
“proper maintenance of mitochondria dynamics, i.e. the balance between fission and fusion, is necessary for optimal muscle mitochondrial function and fitness20–23,43.”
From Disuse-associated loss of the protease Lonp1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass and strength (2022) · cites this paper as [20]
Mfn-1 and -2 deletion in skeletal muscle of young animals leads to abnormal mitochondrial morphology, severe mitochondrial dysfunction, and a severe deficit in muscle growth.
“It was for instance shown in skeletal muscle of young animals that Mfn-1 and -2 deletion leads to abnormal mitochondrial morphology, severe mitochondrial dysfunction, and a severe deficit in muscle growth (Chen et al., 2010).”
From Effects of Aging and Caloric Restriction on Fiber Type Composition, Mitochondrial Morphology and Dynamics in Rat Oxidative and Glycolytic Muscles (2019) · cites this paper as Chen et al., 2010
Mitochondrial fusion apparently allows the mtDNA mutator mouse to carry a higher mutational load without affecting respiratory function.
“Mitochondrial fusion apparently allows the mtDNA mutator mouse to carry a higher mutational load without affecting respiratory function (Chen et al., 2010).”
From Role of the mitochondrial DNA replication machinery in mitochondrial DNA mutagenesis, aging and age-related diseases (2017) · cites this paper as Chen et al., 2010
Conditional deletion of Mfn1 and Mfn2 in mouse skeletal muscle correlates with increased accumulation of mtDNA point mutations and deletions.
“Additionally, conditional deletion of Mfn1 and Mfn2 in mouse skeletal muscle correlates with increased accumulation of mtDNA point mutations and deletions (Chen et al., 2010).”
From Role of the mitochondrial DNA replication machinery in mitochondrial DNA mutagenesis, aging and age-related diseases (2017) · cites this paper as Chen et al., 2010
Depletion of any one of Mfn1, Mfn2 or OPA1 results in severe dysfunction in respiratory capacity and fragmentation of mitochondria.
“Depletion of any of one these proteins results in severe dysfunction in respiratory capacity and fragmentation of mitochondria (Chen et al., 2005; Chen et al., 2010; Song et al., 2009)”
From Role of the mitochondrial DNA replication machinery in mitochondrial DNA mutagenesis, aging and age-related diseases (2017) · cites this paper as Chen et al., 2010
Mitochondrial fusion through intramitochondrial exchange increases the tolerance of a cell to mutant mtDNA and protects the integrity of the mitochondrial genome.
“This study supports the hypothesis that mitochondrial fusion through intramitochondrial exchange increases the tolerance of a cell to mutant mtDNA and protects the integrity of the mitochondrial genome.”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Chen et al., 2010
Muscle-specific Mfn1- and Mfn2-knockout mice have impaired mitochondrial function, abnormal mitochondrial proliferation and muscle loss.
“In a recent study conducted by Chen et al., muscle-specific Mfn1- and Mfn2-knockout mice were reported to have impaired mitochondrial function, abnormal mitochondrial proliferation and muscle loss (Chen et al., 2010).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Chen et al., 2010
Loss of mitochondrial fusion in skeletal muscle results in increased mtDNA point mutations and deletions as well as severe mtDNA depletion, which preceded the phenotypic changes observed in these mutant mice.
“Furthermore, loss of mitochondrial fusion in skeletal muscle resulted in increased mtDNA point mutations and deletions as well as severe mtDNA depletion, which preceded the phenotypic changes observed in these mutant mice.”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Chen et al., 2010
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- Authors
- Chen, H., Vermulst, M., Wang, Y. E., Chomyn, A., Prolla, T. A., McCaffery, J. M., & Chan, D. C.
- Affiliations
- California Institute of Technology (US)
- University of Wisconsin–Madison (US)
- Johns Hopkins University (US)
- Corresponding author
- Chan, David C.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2010-04
- Volume
- 141
- Issue
- 2
- Pages
- 280-289
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC2876819
- OpenAlex
- W2151698573
- Cited by
- 1,211
- References
- 51
- Citations by year
- 2026: 38 · 2025: 65 · 2024: 64 · 2023: 87 · 2022: 86 · 2021: 99 · 2020: 86 · 2019: 76 · 2018: 71 · 2017: 75 · 2016: 75 · 2015: 68 · 2014: 65 · 2013: 78 · 2012: 102
- FWCI
- 32.98
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1239 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of General Medical Sciences (R01GM062967, GM062967)
- National Center for Research Resources (S10RR023454)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- mitochondrial fusion, mitochondrial DNA stability, mitofusins, Mfn1, mitofusin 2, skeletal muscle, mitochondrial DNA mutations, mtDNA depletion, mitochondrial dysfunction, muscle atrophy, mitochondrial proliferation, mitochondrial DNA deletions, conditional knockout mice
- MeSH terms
- DNA Polymerase gamma, Animals, DNA-Directed DNA Polymerase, DNA, Mitochondrial, Embryo, Mammalian, Female, Genes, Lethal, Male, Mitochondria, Muscle, Mutation, Mitochondrial Myopathies, Muscle, Skeletal, GTP Phosphohydrolases, Mitochondrial Proteins, Mice
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