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Fusion and Fission: Interlinked Processes Critical for Mitochondrial Health
Abstract
Mitochondria are dynamic organelles that continually undergo fusion and fission. These opposing processes work in concert to maintain the shape, size, and number of mitochondria and their physiological function. Some of the major molecules mediating mitochondrial fusion and fission in mammals have been discovered, but the underlying molecular mechanisms are only partially unraveled. In particular, the cast of characters involved in mitochondrial fission needs to be clarified. By enabling content mixing between mitochondria, fusion and fission serve to maintain a homogeneous and healthy mitochondrial population. Mitochondrial dynamics has been linked to multiple mitochondrial functions, including mitochondrial DNA stability, respiratory capacity, apoptosis, response to cellular stress, and mitophagy. Because of these important functions, mitochondrial fusion and fission are essential in mammals, and even mild defects in mitochondrial dynamics are associated with disease. A better understanding of these processes likely will ultimately lead to improvements in human health.
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“Fusion and fission are opposing actions that work together to maintain the number, size, shape and function of mitochondria (Chan, 2012).”
From Role of the mitochondrial DNA replication machinery in mitochondrial DNA mutagenesis, aging and age-related diseases (2017) · cites this paper as Chan, 2012
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“Maintaining an optimal balance between mitochondrial fusion and fission is critical for protecting neurons from ROS escalation and facilitating the clearance of damaged organelles through mitophagy [79].”
Mitochondrial dynamics and metastasis
Altieri, D. C. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2961-2 · Cited by 88
Wu, Y., Yao, Y.-M., & Lu, Z. (2019) · Journal of Molecular Medicine · doi:10.1007/s00109-019-01756-2 · Cited by 86
Zhao, Y., Jia, M., Chen, W., & Liu, Z. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.02.021 · Cited by 89
Hammerling, B. C., & Gustafsson, Å. B. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.07.013 · Cited by 86
“Fusion of the inner mitochondrial membranes is driven by the GTPase Opa1 [65].”
InfluentialMechanical ventilation triggers abnormal mitochondrial dynamics and morphology in the diaphragm
Picard, M. A., Azuelos, I., Jung, B., Giordano, C., Matecki, S., Hussain, S. N. A., White, K., Li, T., Liang, F., Benedetti, A., et al. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00873.2014 · Cited by 86
Zhang, T., Mishra, P., Hay, B. A., Chan, D. C., & Guo, M. (2017) · eLife · doi:10.7554/elife.17834 · Cited by 85
“IFM-Gal4, UAS-Mfn RNAi, pCasper-DRP1-HA, PINK15, parkin25, dpk21, parkin25mulA6 were described previously (Clark et al., 2006; Deng et al., 2008; Yun et al., 2014).”
BackgroundInfluentialZhou, L., Zhang, Q., Zhang, P., Sun, L., Peng, C., Yuan, Z., & Cheng, J. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.524 · Cited by 84
“Mitochondria are highly dynamic organelles with continuous fission and fusion that are regulated by several GTPases, such as dynamin-related protein (Drp1) for fission and mitofusin 2 (MFN2) for fusion.(6) Impaired balance of fission and fusion events causes mitochondrial dysfunction and leads to human neurological di…”
BackgroundPascual‐Ahuir, A., Manzanares‐Estreder, S., & Proft, M. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/9860841 · Cited by 87
“Mitochondria form dynamic networks, whose morphology changes in response to stress and nutritional stimuli and damage [150, 151].”
Weil, R., Laplantine, E., Curic, S., & Génin, P. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01243 · Cited by 83
“In mammals, mitochondrial fusion is mediated by mitofusin (Mfn)1 and 2, and optic atrophy 1 (Opa1) belonging to the dynamin GTPases superfamily (6, 7).”
BackgroundChen, M., Gu, Y.-Y., Zhang, A. L., Sze, D., Mo, S., & May, B. H. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105778 · Cited by 83
Xiong, X., Hasani, S., Young, L. E. A., Rivas, D. R., Skaggs, A. T., Martinez, R., Wang, C., Weiss, H. L., Gentry, M. S., Sun, R. C., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00974-5 · Cited by 85
“Mitochondrial dynamics refers to a collection of mitochondrial movements, including continuous cycles of membrane fusion and fission, transporting along the cytoskeleton, and interactions with other organelles [11, 12].”
BackgroundRolland, S. G. M., Motori, E., Memar, N., Hench, J., Frank, S., Winklhofer, K. F., & Conradt, B. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303872110 · Cited by 80
Li, G., Fu, R., Shen, H., Zhou, J., Hu, X., Liu, Y., Li, Y.-N., Zhang, H., Liu, X. B., Zhang, Y.-H., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.14413 · Cited by 83
“Because mitochondrial fragmentation is associated with increases in apoptosis and increased mitochondrial fission parallels the release of Cyto C from the mitochondria into the cytosol in apoptotic cells [33], we next examined the effects of PINK1 knockdown on apoptosis and Cyto C release in polyphyllin I-treated cell…”
BackgroundConnecting mitochondrial dynamics and life-or-death events via Bcl-2 family proteins
Aouacheria, A., Baghdiguian, S., Lamb, H. M., Huska, J. D., Pineda, F. J., & Hardwick, J. M. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.04.009 · Cited by 81
“In mamma ls, Drp1 is responsible for fission, while Mitofusin 1 and 2 (Mfn1/2) and Opa1 carry out fusio n of the mitochondrial outer and inner membranes, respectively (Chan, 2012; van der Bliek et al., 2013).”
Dantas, W. S., Zunica, E. R. M., Heintz, E. C., Vandanmagsar, B., Floyd, Z. E., Yu, Y., Fujioka, H., Hoppel, C. L., Belmont, K. P., Axelrod, C. L., et al. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12982 · Cited by 84
“Mitochondria are dynamic organelles, whose morphology and function are regulated through continuous balancing of fission and fusion processes.(33) For example, genetic ablation or overexpression of DRP1, the primary mediator of mitochondrial fission, impairs skeletal muscle integrity, induces muscle wasting, and dimin…”
BackgroundMIRO GTPases in Mitochondrial Transport, Homeostasis and Pathology
Tang, B. L. (2015) · Cells · doi:10.3390/cells5010001 · Cited by 81
“Other than transport and distribution, mitochondria are dynamic organelles that undergo frequent changes in morphology, as well as fusion and fission [72,73].”
BackgroundMitochondrial Mechanisms of Neuromuscular Junction Degeneration with Aging
Anagnostou, M., & Hepple, R. T. (2020) · Cells · doi:10.3390/cells9010197 · Cited by 84
α-synuclein impairs autophagosome maturation through abnormal actin stabilization
Sarkar, S., Olsen, A. L., Sygnecka, K., Lohr, K. M., & Feany, M. Β. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009359 · Cited by 82
“Since normal mitophagosome formation requires preserved mitochondrial dynamics [22,84], it is possible that excess F-actin stabilization impairs mitophagy through multiple mechanisms in α-synucleinopathy.”
BackgroundThe Emerging Role of MitomiRs in the Pathophysiology of Human Disease
Duarte, F. V., Palmeira, C. M., & Rolo, A. P. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-22671-2_8 · Cited by 83
Váraljai, R., Islam, A. B. M. M. K., Beshiri, M. L., Rehman, J., López-Bigas, N., & Benevolenskaya, E. V. (2015) · Genes & Development · doi:10.1101/gad.264036.115 · Cited by 83
Disruption of SUMO-Specific Protease 2 Induces Mitochondria Mediated Neurodegeneration
Fu, J., Yu, H.-M. I., Chiu, S.-Y., Mirando, A. J., Maruyama, E. O., Cheng, J., & Hsu, W. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004579 · Cited by 80
“Mitochondria possess a highly dynamic nature, undergoing frequent fusion and fission [34].”
BackgroundMitochondrial dynamics: The dynamin superfamily and execution by collusion
Ramachandran, R. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.07.039 · Cited by 81
Mitochondrial function and mitochondrial DNA maintenance with advancing age
Gaziev, A. I., Abdullaev, S., & Podlutsky, A. (2014) · Biogerontology · doi:10.1007/s10522-014-9515-2 · Cited by 77
“Mitochondrial dynamics play a key role in the exchange of components between damaged and functionally active mitochondria (Chan 2012; Otera et al. 2013).”
BackgroundInfluentialExtranuclear SUMOylation in Neurons
Henley, J. M., Carmichael, R. E., & Wilkinson, K. A. (2018) · Trends in Neurosciences · doi:10.1016/j.tins.2018.02.004 · Cited by 81
“Individual mitochondria undergo frequent fusion and fission events as a quality control mechanism [49].”
BackgroundHuman Cytomegalovirus Alters Host Cell Mitochondrial Function during Acute Infection
Combs, J. A., Norton, E. B., Saifudeen, Z. R., zu Bentrup, K. H., Katakam, P. V. G., Morris, C. A., Myers, L., Kaur, A., Sullivan, D. E., & Zwezdaryk, K. J. (2019) · Journal of Virology · doi:10.1128/jvi.01183-19 · Cited by 81
“eration, and numerous other pathologies (14, 22, 23).”
BackgroundMaity, J., Deb, M., Greene, C. J., & Das, H. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101622 · Cited by 76
“Simultaneously, damaged mitochondrial components are sequestered and/or diluted through mitochondrial fission and fusion processes [16].”
BackgroundCharvat, R. A., & Arrizabalaga, G. (2016) · Scientific Reports · doi:10.1038/srep22997 · Cited by 73
“Mammalian cells contain hundreds to thousands of mitochondria, which are maintained through a dynamic process of remodeling to repair or selectively remove damaged mitochondria 67–69 .”
Li, D., Wang, C., Ma, P., Yu, Q., Gu, M., Dong, L., Jiang, W., Pan, S., Xie, C., Han, J., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0494-0 · Cited by 77
Borengasser, S. J., Faske, J., Kang, P., Blackburn, M. L., Badger, T. M., & Shankar, K. (2014) · Physiological Genomics · doi:10.1152/physiolgenomics.00059.2014 · Cited by 76
Mitochondria and sensory processing in inflammatory and neuropathic pain
Ribeiro, P. S. S., Willemen, H. L. D. M., & Eijkelkamp, N. (2022) · Frontiers in Pain Research · doi:10.3389/fpain.2022.1013577 · Cited by 88
MicroRNAs as regulators of mitochondrial function: Role in cancer suppression
Tomasetti, M., Neužil, J., & Dong, L. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.09.002 · Cited by 78
The Gdap1 knockout mouse mechanistically links redox control to Charcot–Marie–Tooth disease
Niemann, A., Huber, N., Wagner, K. M., Somandin, C., Horn, M., Lebrun-Julien, F., Angst, B., Pereira, J. A., Halfter, H., Welzl, H., et al. (2014) · Brain · doi:10.1093/brain/awt371 · Cited by 80
“Different fusion or fission factors of the outer and inner mitochondrial membrane have been identified (Chan, 2012), three of which are also mutated in Charcot–Marie–Tooth disease.”
BackgroundInfluentialThe chaperone co-inducer BGP-15 alleviates ventilation-induced diaphragm dysfunction
Salah, H. A., Li, M., Cacciani, N., Gastaldello, S., Ogilvie, H., Akkad, H., Namuduri, A. V., Morbidoni, V., Artemenko, K. A., Balogh, G. E., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf7099 · Cited by 76
Metadata
- Authors
- Chan, D. C.
- Affiliations
- California Institute of Technology (US)
- Corresponding author
- Chan, David C.
- ORCID
- Chan, David C.
- Venue
- Annual Review of Genetics
- Publisher
- Annual Reviews
- Published
- 2012-12-15
- Volume
- 46
- Issue
- 1
- Pages
- 265-287
- ISSN
- 0066-4197 (ISSN-L)
- 1545-2948
- OpenAlex
- W2157334943
- Cited by
- 1,196
- References
- 141
- Citations by year
- 2026: 56 · 2025: 45 · 2024: 73 · 2023: 97 · 2022: 94 · 2021: 109 · 2020: 110 · 2019: 102 · 2018: 96 · 2017: 93 · 2016: 89 · 2015: 100 · 2014: 76 · 2013: 53 · 2012: 2
- FWCI
- 3.80
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Genetics (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM062967, GM083121, GM062967, R01GM083121)
- 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, mitochondrial dynamics, mitochondrial morphology, mitochondrial DNA stability, respiratory capacity, apoptosis, cellular stress response, mitophagy, mitochondrial disease
- MeSH terms
- Animals, DNA, Mitochondrial, Humans, Membrane Proteins, Mitochondria, Mitosis, Mutation, Apoptosis, GTP Phosphohydrolases, Mitochondrial Diseases, Dynamins, Mitochondrial Membranes, Mice, Mitochondrial Size, Mitochondrial Turnover
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