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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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“These cues regulate mitochondrial shape, number, and size, as well as the ability to meet demand for cellular energy (Chan 2012).”
BackgroundInfluentialTwo separate functions of NME3 critical for cell survival underlie a neurodegenerative disorder
Chen, C., Wang, H., Huang, C.-W., Huang, C.-Y., Lim, W. K., Tu, I.-C., Koorapati, A., Hsieh, S., Kan, H., Tzeng, S., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1818629116 · Cited by 56
“In humans, the fusion and fission processes require four dynamin-related GTPases: MFN1, MFN2, OPA1, and DRP1.”
BackgroundInfluentialZhang, H., Pan, Z., Ju, J., Xing, C., Li, X., Shan, M., & Sun, S. (2020) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-020-00489-4 · Cited by 60
“central domain and a C-terminal GTPase effector domain in addition to its N-terminal GTPase [8].”
BackgroundThe Role of Mitochondrial Dynamic Dysfunction in Age-Associated Type 2 Diabetes
Vezza, T., Díaz-Pozo, P., Canet, F., de Marañón, A. M., Abad-Jiménez, Z., García-Gargallo, C., Roldan, I., Solá, E., Bañuls, C., López‐Domènech, S., et al. (2022) · The World Journal of Men s Health · doi:10.5534/wjmh.210146 · Cited by 59
“In cultured cells, inhibition of mitochondrial fusion has been shown to reduce mtDNA, mtDNA-encoded proteins and membrane integrity, consequently altering oxidative phosphorylation, since fusion-deficient mitochondria cannot exchange their contents [37].”
BackgroundMitochondrial synapses: intracellular communication and signal integration
Picard, M. A. (2015) · Trends in Neurosciences · doi:10.1016/j.tins.2015.06.001 · Cited by 58
Losón, O. C., Meng, S., Ngo, H., Liu, R., Kaiser, J. T., & Chan, D. C. (2015) · Protein Science · doi:10.1002/pro.2629 · Cited by 57
Mitochondrial regulation of diabetic vascular disease: an emerging opportunity
Widlansky, M. E., & Hill, R. B. (2018) · Translational research · doi:10.1016/j.trsl.2018.07.015 · Cited by 58
Vantaggiato, C., Castelli, M., Giovarelli, M., Orso, G., Bassi, M. T., Clementi, E., & Palma, C. D. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00120 · Cited by 57
“Three large GTPases are involved in mitochondrial fusion: Mitofusins 1 and 2 (Mfn1 and Mfn2), that mediate outer mitochondrial membrane fusion, and Optic atrophy 1 protein (Opa1), the mediator of inner-membrane fusion (Chan, 2012).”
BackgroundKirov, S. A., Fomitcheva, I. V., & Sword, J. (2020) · Cerebral Cortex · doi:10.1093/cercor/bhaa134 · Cited by 57
The MFN1 and MFN2 mitofusins promote clustering between mitochondria and peroxisomes
Huo, Y., Sun, W., Shi, T., Gao, S., & Zhuang, M. (2022) · Communications Biology · doi:10.1038/s42003-022-03377-x · Cited by 59
Rice bran extract improves mitochondrial dysfunction in brains of aged NMRI mice
Hagl, S., Berressem, D., Grewal, R., Sus, N., Frank, J., & Eckert, G. P. (2015) · Nutritional Neuroscience · doi:10.1179/1476830515y.0000000040 · Cited by 56
How to get out: ssRNA enveloped viruses and membrane fission
Weissenhorn, W., Poudevigne, E., Effantin, G., & Bassereau, P. M. (2013) · Current Opinion in Virology · doi:10.1016/j.coviro.2013.03.011 · Cited by 61
“Dynamin has been also implicated in the budding of caveolae [11] and dynamin-like molecules catalyze mitochondrial fission [12].”
Chuang, Y.-C., Liou, C., Chen, S., Wang, P., Chuang, J., Tiao, M., Hsu, T., Lin, H., & Lin, T. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/5691215 · Cited by 58
“In mammalian cells, dynamin 1-like (DNM1L or DRP1), mitochondrial fission factor (MFF), and fission 1 (FIS1) are involved in the fission process, while optic atrophy 1 (OPA1) and mitofusin 1 and 2 (MFN1 and MFN2) participate in the fusion process [11].”
BackgroundLan, B., He, Y., Sun, H., Zheng, X., Gao, Y., & Li, N. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.116587 · Cited by 58
Zhou, B., Fang, L., Dong, Y., Yang, J., Chen, X., Zhang, N., Zhu, Y., & Huang, T. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03660-5 · Cited by 56
Therapeutic applications of mitochondrial transplantation
Ülger, Ö., & Kubat, G. B. (2022) · Biochimie · doi:10.1016/j.biochi.2022.01.002 · Cited by 56
Mitochondrial fragmentation and ROS signaling in wound response and repair
Xu, S., Li, S., Björklund, M., & Xu, S. (2022) · Cell Regeneration · doi:10.1186/s13619-022-00141-8 · Cited by 58
“These morphologies are controlled by antagonizing fusion and fission events (Chan 2012).”
BackgroundJoshi, D. C., Chavan, M. B., Gurow, K., Gupta, M., Dhaliwal, J. S., & Ming, L. C. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.117827 · Cited by 62
Mitochondrial protein quality control in health and disease
Baker, M. J., Palmer, C. S., & Stojanovski, D. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12430 · Cited by 60
“At the organelle level, mitochondria are highly dynamic and constantly undergo fission and fusion events (Westermann, 2010; Chan, 2012; Elgass et al., 2013).”
BackgroundMitochondrial dynamics: biology and therapy in lung cancer
Lennon, F. E., & Salgia, R. (2014) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2014.899350 · Cited by 55
“Optic atrophy protein-1 (OPA1) Fusion Inner membrane fusion, possible role in apoptotic resistance Inner mitochondrial membrane [35,52,72,73] F.”
BackgroundInfluentialDistinct functional determinants of influenza hemagglutinin-mediated membrane fusion
Ivanovic, T., & Harrison, S. C. (2015) · eLife · doi:10.7554/elife.11009 · Cited by 55
“Published data on fusion inhibition by antibodies to the ’stem’ of influenza virus hemagglutinin (HA) now allow us to incorporate into simulations the provision that some HAs are inactive.”
BackgroundThe secret messages between mitochondria and nucleus in muscle cell biology
Soledad, R. B., Charles, S., & Das, S. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.03.019 · Cited by 54
miR-214 represses mitofusin-2 to promote renal tubular apoptosis in ischemic acute kidney injury
Yu, Y., Ma, Z., Zhu, J., Zeng, M., Liu, H., & Dong, Z. (2020) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00567.2019 · Cited by 55
Wu, X., Cui, W., Guo, W., Liu, H., Luo, J., Zhao, L., Guo, H., Zheng, L., Bai, H., Feng, D., et al. (2020) · Neuroscience Bulletin · doi:10.1007/s12264-020-00505-7 · Cited by 55
“However, the post-translational modifications of Drp1 which regulate its recruitment to mitochondria are a complicated process, including not only phosphorylation, but also S-nitrosilation, ubiquitination, and sumoylation [27, 45, 46].”
BackgroundQuinn, K. M., Hussain, T., Kraus, F., Formosa, L. E., Lam, W. K., Dagley, M. J., Saunders, E. C., Assmus, L. M., Wynne-Jones, E., Loh, L., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16633-7 · Cited by 56
The role of mitochondrial dynamics in mtDNA maintenance
Sabouny, R., & Shutt, T. E. (2021) · Journal of Cell Science · doi:10.1242/jcs.258944 · Cited by 51
Qin, X., Wang, R., Xu, H., Tu, L., Chen, H., Li, H., Liu, N., Wang, J., Li, S., Yin, F., et al. (2022) · Autophagy · doi:10.1080/15548627.2021.2022360 · Cited by 55
“mechanism of Q14-induced mitochondrial fragmentation, we next investigated the effect of Q14 peptide on key mitochondrial fusion and fission factors [50,51].”
BackgroundParkin Overexpression Attenuates Sepsis-Induced Muscle Wasting
Leduc-Gaudet, J.-P., Mayaki, D., Reynaud, O., Broering, F. E., Chaffer, T. J., Hussain, S. N. A., & Gouspillou, G. (2020) · Cells · doi:10.3390/cells9061454 · Cited by 54
“, morphology), size and number of mitochondria [41,49].”
BackgroundResult
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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