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Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction
Open accessAbstract
Mitochondria undergo continual cycles of fusion and fission, and the balance of these opposing processes regulates mitochondrial morphology. Paradoxically, cells invest many resources to maintain tubular mitochondrial morphology, when reducing both fusion and fission simultaneously achieves the same end. This observation suggests a requirement for mitochondrial fusion, beyond maintenance of organelle morphology. Here, we show that cells with targeted null mutations in Mfn1 or Mfn2 retained low levels of mitochondrial fusion and escaped major cellular dysfunction. Analysis of these mutant cells showed that both homotypic and heterotypic interactions of Mfns are capable of fusion. In contrast, cells lacking both Mfn1 and Mfn2 completely lacked mitochondrial fusion and showed severe cellular defects, including poor cell growth, widespread heterogeneity of mitochondrial membrane potential, and decreased cellular respiration. Disruption of OPA1 by RNAi also blocked all mitochondrial fusion and resulted in similar cellular defects. These defects in Mfn-null or OPA1-RNAi mammalian cells were corrected upon restoration of mitochondrial fusion, unlike the irreversible defects found in fzodelta yeast. In contrast, fragmentation of mitochondria, without severe loss of fusion, did not result in such cellular defects. Our results showed that key cellular functions decline as mitochondrial fusion is progressively abrogated.
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“fibroblasts lacking Mfn1 and Mfn2 completely lack mitochondrial fusion and show severe cellular defects, including poor growth, heterogeneity of mitochondrial membrane potential, and decreased respiration (11).”
From Mitochondrial Fission Contributes to Mitochondrial Dysfunction and Insulin Resistance in Skeletal Muscle (2012) · cites this paper as [11]
In the citing paper
“This is of particular importance since it is now established that mitochondrial morphology and function are interrelated, with changes in mitochondrial morphology affecting mitochondrial function (Chen et al., 2005; Jahani-Asl et al., 2007; Yu et al., 2008; Ong et al., 2010; Gomes et al., 2011) and vice versa (Benard et al., 2007).”
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., 2005
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“Repression of Mfn2 in cells decreases oxygen consumption, glucose oxidation, mitochondrial membrane potential and the expression of oxidative phosphorylation proteins (Bach et al., 2003; Chen et al., 2005; Pich et al., 2005).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Chen et al., 2005
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“…mitochondrial complementation (via fusion) suppresses mtDNA disease-associated alleles in various mouse tissues (Nakada et al., 2001), and loss of mitochondrial fusion increases mitochondrial heterogeneity and dysfunctional mitochondrial units in mouse embryonic fibroblasts (H. Chen et al., 2005).”
MIRO‐1 interacts with VDAC‐1 to regulate mitochondrial membrane potential in Caenorhabditis elegans
Ren, X., Zhou, H., Sun, Y., Fu, H., Ran, Y., Yang, B., Yang, F., Björklund, M., & Xu, S. (2023) · EMBO Reports · doi:10.15252/embr.202256297 · Cited by 19
“Mouse embryonic fibroblasts (MEFs) that lack MFN1/2 suffer from reduced respiratory capacity but also experience a seemingly stochastic loss of D Ψ m (Chen et al , 2005).”
Tarallo, D., Martínez, J., Leyva, A., Mónaco, A., Perroni, C., Tassano, M. R., Gambini, J. P., Cappetta, M., Durán, R., Moreno, M., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-51427-7 · Cited by 20
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“Disruption of either fusion process due to loss of mitofusins or OPA1 [9] or fission process due to loss of Drp1 have been shown to result in cellular dysfunction, reduced respiration, loss of mitochondrial membrane potential and growth inhibition [9,10].”
Upadhyay, M., Agarwal, S., Bhadauriya, P., & Ganesh, S. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.01.002 · Cited by 20
“The mitofusins Mfn1/2 and OPA1 (gene mutated in dominant optic atrophy) regulate the fusion (Chen et al., 2005; Cipolat et al., 2004) while DRP1 (dynamin-related protein) regulates the fission (Smirnova et al., 2001).”
BackgroundMitochondrialne kanały potasowe: podsumowanie
Szewczyk, A. M., Bednarczyk, P., Jędraszko, J., Kampa, R. P., Koprowski, P., Krajewska, M., Kucman, S. K., Kulawiak, B., Laskowski, M., Rotko, D., et al. (2018) · Postępy Biochemii · doi:10.18388/pb.2018_132 · Cited by 21
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“Therefore, the aberrant mitochondrial dynamics result in the impaired bioenergetics, excessive generation of reactive oxygen species (ROS), loss of mitochondrial membrane potential, dysfunction of endogenous respiration and the release of pro-apoptotic factors from mitochondria, which trigger cell death (Morris and Ho…”
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“In contrast, Mfn2-mutant cells exhibit mitochondrial spheres of widely varying sizes ( 5, 8 ).”
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Huang, W., Jou, M., & Tsung, I. P. (2014) · PLoS ONE · doi:10.1371/annotation/c85feb29-046d-45f6-ba12-510f9e1d9412 · Cited by 20
Luo, T., Liu, H., Chen, B., Liu, H., Abdel‐Latif, A., Kitakaze, M., Wang, X., Wu, Y., Chou, D., & Kim, J. K. (2021) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2021.03.021 · Cited by 19
Stein, J., Walkenfort, B., Cihankaya, H., Hasenberg, M., Bader, V., Winklhofer, K. F., Röderer, P., Matschke, J., Theiß, C., & Matschke, V. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6924251 · Cited by 21
“Thus, the cell implies mitochondrial fi ssion processes to generate small mitochondria that can be more easily degraded [48 – 51].”
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“Mitochondrial dynamics, including fusion and division, contribute to the mitochondrial respiratory chain and ROS scavenging [17].”
BackgroundPark, S., Cha, H.-N., Shin, M., Park, S., Kim, Y., Kim, M., Shin, K., Thoudam, T., Lee, E. J., Wolfe, R. R., et al. (2024) · Diabetes · doi:10.2337/db23-0432 · Cited by 19
Relationships Between Mitochondrial Dynamics and Bioenergetics
Bénard, G., Bellancé, N., José, C., & Rossignol, R. (2011) · Springer eBooks · doi:10.1007/978-94-007-1291-1_2 · Cited by 24
“The downregulation of OPA1 expression in human cells, or the occurence of pathogenic mutations in this protein are associated with an alteration of OXPHOS functioning (Chen et al. 2005; Chevrollier et al. 2008; Olichon et al. 2003).”
BackgroundAbcc9 is required for the transition to oxidative metabolism in the newborn heart
Fahrenbach, J. P., Stoller, D. A., Kim, G. H., Aggarwal, N. T., Yerokun, B. A., Earley, J. U., Hadhazy, M., Shi, N., Makielski, J. C., & McNally, E. M. (2014) · The FASEB Journal · doi:10.1096/fj.13-244459 · Cited by 19
“The down-regulation of mitofusin 2 suggests that Ex5 mitochondria have a fusion defect that may contribute to the lower cellular respiration (34, 35).”
BackgroundLonghi, R., Almeida, R. F., Pettenuzzo, L. F., de Souza, D. G., Machado, L. D. S., Quincozes‐Santos, A., & Souza, D. O. (2017) · European Journal of Nutrition · doi:10.1007/s00394-017-1474-3 · Cited by 18
Ryan, Z. C., Craig, T. A., Wang, X., Delmotte, P. F., Salisbury, J. L., Lanza, I. R., Sieck, G. C., & Kumar, R. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.01.092 · Cited by 19
“mediator of mitochondrial fission [34,39,40] and the reduced expression of mRNAs for the mitochondrial fusion mediators, OPA1 and MFN2 [35,41,42] might account for the increase in mitochondrial fragmentation.”
BackgroundExercise and Mitochondrial Remodeling in Skeletal Muscle in Type 2 Diabetes
Lee, H., & Song, W. J. (2018) · Journal of Obesity & Metabolic Syndrome · doi:10.7570/jomes.2018.27.3.150 · Cited by 26
The second genome: Effects of the mitochondrial genome on cancer progression
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The ubiquitous role of mitochondria in Parkinson and other neurodegenerative diseases
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“OPA1 deficiency leads to alterations of cristae structure and fusion impairment in cells [15, 16].”
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Contribution of mitochondria to pain in diabetic neuropathy
Hernández-Beltrán, N., Moreno, C. B., & Gutiérrez‐Álvarez, Á. M. (2013) · Endocrinología y Nutrición (English Edition) · doi:10.1016/j.endoen.2013.01.004 · Cited by 19
Newman, L. E., Schiavon, C. R., Zhou, C., & Kahn, R. (2017) · PLoS ONE · doi:10.1371/journal.pone.0175164 · Cited by 20
“MFN1 and MFN2 regulate outer membrane fusion [6, 7], and OPA1 promotes inner membrane fusion [8].”
BackgroundResultInfluentialSommers, O., Tomsine, R. A., & Khacho, M. (2024) · Cells · doi:10.3390/cells13211773 · Cited by 22
HSF-1 promotes longevity through ubiquilin-1-dependent mitochondrial network remodelling
Erinjeri, A. P., Wang, X., Williams, R., Chiozzi, R. Z., Thalassinos, K., & Labbadia, J. P. (2024) · Nature Communications · doi:10.1038/s41467-024-54136-x · Cited by 20
López-Molina, L., Pereda-Velarde, A., Franco, N. D., Aerts, I., Sebastiá, E. M., Valls‐Roca, L., Guitart‐Mampel, M., Garrabou, G., & Ginés, S. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02341-6 · Cited by 23
“Particularly, changes in mitochondrial metabolism and energy production can directly or indirectly influence fission and fusion rates by modulating ATP, GTP levels, and associated signaling cascades [65, 66].”
Engelhart, E. A., & Hoppins, S. C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006347 · Cited by 19
“Mfn1-null MEFs have a fragmented mitochondrial network characterized by short, rod-shaped mitochondria due to low rates of mitochondrial fusion (14, 33).”
BackgroundLactate metabolism is essential in early-onset mitochondrial myopathy
Chen, Z., Bordieanu, B., Kesavan, R., Lesner, N. P., Venigalla, S. S. K., Shelton, S. D., DeBerardinis, R. J., & Mishra, P. (2023) · Science Advances · doi:10.1126/sciadv.add3216 · Cited by 18
“Mitochondrial fusion is required for maintenance of the mitochondrial genome, and genetic co-deletion of Mfn1 and Mfn2 results in severe reduction in mtDNA quantity and quality in both cultured cells and muscle tissue ( 19 , 20 ).”
Makiuchi, T., Santos, H. J., Tachibana, H., & Nozaki, T. (2017) · Scientific Reports · doi:10.1038/s41598-017-13721-5 · Cited by 18
The single mitochondrion of the kinetoplastid parasite Crithidia fasciculata is a dynamic network
DiMaio, J., Ruthel, G. T., Cannon, J. J., Malfara, M. F., & Povelones, M. L. (2018) · PLoS ONE · doi:10.1371/journal.pone.0202711 · Cited by 16
“Fusion homogenizes proteins and other macromolecules which is important for overall mitochondrial health and network function [11-14].”
Background
Metadata
- Authors
- Chen, H., Chomyn, A., & Chan, D. C.
- Affiliations
- California Institute of Technology (US)
- Corresponding author
- Chan, David C.
- ORCID
- Chan, David C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-07
- Volume
- 280
- Issue
- 28
- Pages
- 26185-26192
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2124140045
- Cited by
- 1,376
- References
- 28
- Citations by year
- 2026: 32 · 2025: 53 · 2024: 55 · 2023: 61 · 2022: 63 · 2021: 77 · 2020: 84 · 2019: 79 · 2018: 95 · 2017: 89 · 2016: 56 · 2015: 74 · 2014: 78 · 2013: 70 · 2012: 92
- FWCI
- 15.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- Muscular Dystrophy Association
- United Mitochondrial Disease Foundation
- National Institutes of Health
- National Institute of General Medical Sciences (GM11726, 1 R01 GM62967-01, R01GM062967)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- mitochondrial fusion, mitochondrial fission, Mfn1, mitofusin 2, OPA1, mitochondrial heterogeneity, mitochondrial membrane potential, cellular respiration, mitochondrial morphology, mitochondrial dysfunction
- MeSH terms
- Alleles, Animals, Fibroblasts, Genotype, Membrane Potentials, Microscopy, Fluorescence, Mitochondria, Mutation, Oxygen, Oxygen Consumption, Polyethylene Glycols, Recombinant Fusion Proteins, RNA, Time Factors, Blotting, Western, Microscopy, Confocal, GTP Phosphohydrolases, RNA Interference, Cell Proliferation, Green Fluorescent Proteins, Mice
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