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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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Central Parkin: The evolving role of Parkin in the heart
Dorn, G. W. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.014 · Cited by 30
“Although there are differences in GTPase activities, these two proteins are highly similar (63% identity and 80% conserved amino acid sequence), have overlapping functions and mutually interact to promote mitochondrial fusion [32].”
BackgroundQuarato, E. R., Salama, N., Li, A. J., Smith, C. O., Zhang, J., Kawano, Y., McArthur, M. J., Liesveld, J. L., Becker, M. W., Elliott, M. R., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05931-9 · Cited by 31
Buonfiglio, F., Korb, C. A., Stoffelns, B. M., Pfeiffer, N., & Gericke, A. (2024) · Aging and Disease · doi:10.14336/ad.2024.0124 · Cited by 35
“Imbalanced mitochondrial fission/fusion may disturb the motility and ATP synthesis in mitochondria, promote ROS generation and mtDNA mutations, and further affect intracellular Ca²⁺ concentration, inevitably leading to cell death [162, 245, 246].”
3 D Mitochondrial Structure in Aging Human Skeletal Muscle: Insights Into MFN ‐2‐Mediated Changes
Scudese, E., Marshall, A. G., Vue, Z., Exil, V. J., Rodriguez, B. I., Demirci, M., Vang, L., Lopez, E. G., Neikirk, K., Shao, B., et al. (2025) · Aging Cell · doi:10.1111/acel.70054 · Cited by 32
“Interruptions of either of these processes can interfere with mitochondrial function, cause dysfunction, and be representative of pathology (Chan 2012; Bartsakoulia et al. 2018; Chen et al. 2005).”
Khoo, N. K. H., Mo, L., Zharikov, S. I., Kamga, C., Quesnelle, K. M., Golin-Bisello, F., Li, L., Wang, Y., & Shiva, S. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.02.009 · Cited by 32
Wang, J., Cai, J., Huang, Y., Ke, Q., Wu, B., Wang, S., Han, X., Wang, T., Wang, Y., Li, W., et al. (2015) · Oncogene · doi:10.1038/onc.2015.370 · Cited by 30
Low mitochondrial activity within developing earthworm male germ-line cysts revealed by JC-1
Małota, K., Student, S., & Świątek, P. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.01.007 · Cited by 30
Cooper, H. A., & Eguchi, S. (2018) · Clinical Science · doi:10.1042/cs20180671 · Cited by 30
RetractedWhy don't mice lacking the mitochondrial Ca2+ uniporter experience an energy crisis?
Wang, P., Fernández‐Sanz, C., Wang, W., & Sheu, S. (2018) · The Journal of Physiology · doi:10.1113/jp276636 · Cited by 29
“One of the potential mechanisms is mitochondrial dynamics, which refers to the changes in mitochondrial morphology including fission, fusion and movement (Chan, 2012; Friedman & Nunnari, 2014).”
BackgroundQin, W., Tong, X., Liang, R., Tang, K., Wu, X., Jia, Y., & Tan, N. (2021) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2021.113827 · Cited by 30
Mao, X., Gu, Y., Sui, X., Shen, L., Han, J. S., Wang, H., Xi, Q., Zhuang, Q., Meng, Q., & Wu, G. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.673618 · Cited by 35
“The mitochondrion is a highly dynamic organelle that undergoes fuse and division under physiological conditions (Chan, 2012).”
BackgroundDefining Mitochondrial Cristae Morphology Changes Induced by Aging in Brown Adipose Tissue
Crabtree, A., Neikirk, K., Marshall, A. G., Vang, L., Whiteside, A. J., Williams, Q., Altamura, C. T., Owens, T. C., Stephens, D. C., Shao, B., et al. (2023) · Advanced Biology · doi:10.1002/adbi.202300186 · Cited by 31
Rojas-Charry, L., Cookson, M., Niño, A., Arboleda, H., & Arboleda, G. (2014) · NeuroToxicology · doi:10.1016/j.neuro.2014.04.007 · Cited by 29
“Some studies have shown that Opa1 and mitofusins act at different steps of the fusion process since Opa1 knockout MEFs maintain fusion of the outer membrane but their inner membranes do not fuse (Chan, 2012).”
BackgroundThe mitochondrial Ras-related GTPase Miro: views from inside and outside the metazoan kingdom
Yamaoka, S., & Hara‐Nishimura, I. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00350 · Cited by 30
Wigington, C. P., Morris, K. J., Newman, L. E., & Corbett, A. H. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.754069 · Cited by 30
“Although mitochondrial fragmentation results from an imbalance of mitochondrial fission and fusion and these are coupled to energy metabolism, regulation of these processes remains an active area of research (89, 90).”
BackgroundZhang, S., Yang, C., Yang, Z., Zhang, D., Ma, X., Mills, G. B., & Liu, Z. (2015) · Europe PMC (PubMed Central) · Cited by 29
RetractedSalvianolic acid B inhibits mitochondrial dysfunction by up-regulating mortalin
Liu, Y., Hu, Y., Qiukai, E., Zuo, J., Yang, L., & Liu, W. (2017) · Scientific Reports · doi:10.1038/srep43097 · Cited by 29
Regulation of mitochondrial quality following repeated bouts of hindlimb unloading
Rosa‐Caldwell, M. E., Brown, J. L., Perry, R. A., Shimkus, K. L., Shirazi‐Fard, Y., Brown, L. A., Hogan, H. A., Fluckey, J. D., Washington, T. A., Wiggs, M. P., et al. (2019) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2019-0218 · Cited by 30
“Fission, mediated by mitochondrial regulatory signals (FIS1, DRP1, and MFF), is the removal of mitochondrial components from the mitochondrial network (typically for subsequent autophagic removal); whereas fusion of mitochondrial networks (mediated by MFN1, MFN2, and OPA1) allows for efficient sharing of mitochondrial…”
BackgroundWang, W., Wang, M., Ruan, Y., Tan, J., Wang, H., Yang, T., Li, J., & Zhou, Q. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b04178 · Cited by 29
Power Failure of Mitochondria and Oxidative Stress in Neurodegeneration and Its Computational Models
Woo, J., Cho, H., Seol, Y., Kim, S. H., Park, C., Yousefian-Jazi, A., Hyeon, S. J., Lee, J.-H., & Ryu, H. (2021) · Antioxidants · doi:10.3390/antiox10020229 · Cited by 32
“Whereas dynaminrelated protein1 (Drp1) and fission1 (Fis1) promote mitochondrial fission (Figure 2B,C) [51].”
BackgroundThe Uprising of Mitochondrial DNA Biomarker in Cancer
Khair, S. Z. N. M., Radzak, S. M. A., & Yusoff, A. A. M. (2021) · Disease Markers · doi:10.1155/2021/7675269 · Cited by 29
Mitofusin 2, a key coordinator between mitochondrial dynamics and innate immunity
Kim, I. S., Silwal, P., & Jo, E. (2021) · Virulence · doi:10.1080/21505594.2021.1965829 · Cited by 29
“These proteins are essential for mitochondrial quality control and homeostasis, as well as the regulation of numerous biological processes, including immune responses [6,7].”
BackgroundMyocardial Infarction as a Consequence of Mitochondrial Dysfunction
Wal, P., Aziz, N., Singh, Y. K., Wal, A., Kosey, S., & Rai, A. K. (2023) · Current Cardiology Reviews · doi:10.2174/1573403x19666230508114311 · Cited by 33
Mitochondria and Reactive Oxygen Species Contribute to Neurogenic Hypertension
Chan, S. H. H., & Chan, J. Y. H. (2017) · Physiology · doi:10.1152/physiol.00006.2017 · Cited by 30
“shape changes involving fusion and fission from an elongated tubular structure to fragmented independent organelles (20).”
BackgroundMethamphetamine-induced dopaminergic neurotoxicity as a model of Parkinson’s disease
Shin, E., Jeong, J. H., Hwang, Y., Sharma, N., Dang, D., Nguyen, B.-T., Nah, S.-Y., Jang, C., Bing, G., Nabeshima, T., et al. (2021) · Archives of Pharmacal Research · doi:10.1007/s12272-021-01341-7 · Cited by 31
“2009; Chan 2012).”
Megamitochondria plasticity: Function transition from adaption to disease
Shang, Y., Li, Z., Cai, P., Li, W., Xu, Y., Zhao, Y., Xia, S., Shao, Q., & Wang, H. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.06.001 · Cited by 28
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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