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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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“Mitochondrial dynamics serve as a crucial quality control mechanism for retaining the mitochondrial population, which is essential for the stability of mitochondrial DNA, respiratory efficiency, and cellular stress response (Chan 2012).”
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Thapliyal, S., Namdar, H. K., McMillan, R. K., Afolabi, J., Marshall, A. G., Venkhatesh, P., Pujala, R. K., Hinton, A. O., Jr., Parry, H. A., Glancy, B. C., et al. (2026) · Current Protocols · doi:10.1002/cpz1.70324 · Cited by 2
Mitochondria in muscle stem cell biology: gatekeepers of fate, function, and regeneration
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“Mitochondrial fusion, regulated by Mitofusin 1/2 (MFN1/2) for outer membrane integration and by optic atrophy 1 (OPA1) for inner membrane maintenance, facilitates mitochondrial genome integration, preservation of membrane potential, and enhanced capacity for OXPHOS [46, 47].”
Dong, J., Zhang, X., Liu, X., Peng, D., Jing, J., Xu, S., Yang, Q., Han, Y., LIU, Y. F., Li, H., et al. (2026) · Cellular Signalling · doi:10.1016/j.cellsig.2026.112578 · Cited by 2
Zeinsteger, P. A., Barberón, J. L., Leaden, P. J., & Palacios, A. (2018) · Medicinal Chemistry Research · doi:10.1007/s00044-018-2254-1 · Cited by 2
“Such studies are important considering that injured mitochondria are associated with cell death and consequent tissue alterations in many pathological processes of different organs (Chan 2012; Du et al. 2012).”
BackgroundOxidative Stress, Metabolism and Photoaging – The Role of Mitochondria
Jackson, M. J., Naidoo, K., & Birch‐Machin, M. A. (2019) · Royal Society of Chemistry eBooks · doi:10.1039/9781788015981-00105 · Cited by 2
Panda, A., Kobzev, D., Кулык, О. Г., Bazylevich, A., Gellerman, G., & Patsenker, L. D. (2023) · Dyes and Pigments · doi:10.1016/j.dyepig.2023.111648 · Cited by 2
Periodic ethanol supply as a path toward unlimited lifespan of Caenorhabditis elegans dauer larvae
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“…have been omitted in the original model Kaptan et al. (2020) while having potential for lifespan extension: detoxi fi cation Xu et al. (2005); Chen (2011) and a possibility for mitochondria to regenerate Palikaras and Tavernarakis (2014); Ni et al. (2015); Chan (2012) (see green arrows in Figure 2).”
Serine 39 in the GTP ‐binding domain of Drp1 is involved in shaping mitochondrial morphology
Ghani, M., Szabó, B., Alkhatibe, M., Amsalu, H., Peleg, Z., Janka, E. A., Mótyán, J. A., & Tar, K. (2024) · FEBS Open Bio · doi:10.1002/2211-5463.13820 · Cited by 2
“Several of these proteins have been identified, including the mitochondrial fission protein (Fis1), mitochondrial dynamic proteins of 49 and 51 kDa (MiD 49, MiD51), and the mitochondrial fis-sion factor (MFF) [13].”
BackgroundShyam, H., Jain, M., Pandey, A. K., & Kumar, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-23881-9.00006-2 · Cited by 2
Cao, C., Lü, J., Lu, P., Li, L., Zhang, F., Li, X., Chen, G., Bai, L., & Li, H. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149455 · Cited by 2
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Prevalence of antimitochondrial antibodies in autism spectrum subjects
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Review on Exercise and Mitochondrial Dynamics
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Energy-Redox Axis in Mitochondria: Interconnection of Energy-Transducing Capacity and Redox Status
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Priyanka, A., Nair, A., Anusree, S. S., Nisha, V. M., & Raghu, K. G. (2016) · RSC Advances · doi:10.1039/c6ra22298f · Cited by 2
Introductory Chapter: Mitochondrial Alterations and Neurological Disorders
Balogiannis, S. (2020) · IntechOpen eBooks · doi:10.5772/intechopen.91051 · Cited by 2
“In addition, Opa1, which is a GTPase, demonstrating dynaminlike properties, plays a substantial role in the modulation of the cristae structure and in their remodeling during mitochondrial fusion and fission [44] and apoptotic process [45].”
BackgroundIs Space the Final Frontier for Mitochondrial Study?
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Naderi, N., Ebadi, B., Damirchi, A., Alamdari, K. A., & Darbandi-Azar, A. (2018) · Research in Cardiovascular Medicine · doi:10.4103/rcm.rcm_11_18 · Cited by 2
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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