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Mitochondrial fusion and fission: The fine‐tune balance for cellular homeostasis
Open accessAbstract
Mitochondria are highly dynamic, maternally inherited cytoplasmic organelles, which fulfill cellular energy demand through the oxidative phosphorylation system. Besides, they play an active role in calcium and damage‐associated molecular patterns signaling, amino acid, and lipid metabolism, and apoptosis. Thus, the maintenance of mitochondrial integrity and homeostasis is extremely critical, which is achieved through continual fusion and fission. Mitochondrial fusion allows the transfer of gene products between mitochondria for optimal functioning, especially under metabolic and environmental stress. On the other hand, fission is crucial for mitochondrial division and quality control. The imbalance between these two processes is associated with various ailments such as cancer, neurodegenerative and cardiovascular diseases. This review discusses the molecular mechanisms that control mitochondrial fusion and fission and how the disruption of mitochondrial dynamics manifests into various disease conditions.
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“Oxidative stress leads to oxidative damage to biomolecules (especially DNA),201 causing endogenous damage-associated molecular patterns (DAMPs) production and cytokine release in the organism.202,203”
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“Cytokines activate downstream signaling pathways of pattern recognition receptors,203 causing systemic chronic inflammatory responses in the body.204”
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Cites
Endothelial Cell Dysfunction and the Pathobiology of Atherosclerosis
Gimbrone, M. A., & García‐Cardeña, G. (2016) · Circulation Research · doi:10.1161/circresaha.115.306301 · Cited by 3,694
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
ER Tubules Mark Sites of Mitochondrial Division
Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072
Mitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
Gomes, L. C., Benedetto, G. D., & Scorrano, L. (2011) · Nature Cell Biology · doi:10.1038/ncb2220 · Cited by 1,735
Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572
Mitochondrial Dynamics and Its Involvement in Disease
Chan, D. C. (2020) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-012419-032711 · Cited by 1,416
Mitochondrial dynamics: overview of molecular mechanisms
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397
Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction
Chen, H., Chomyn, A., & Chan, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503062200 · Cited by 1,376
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Ayyappan, P., Gandy, T. C. T., Sturdevant, D. A., Larsen, T. D., Mukuntharaj, P., Paulson, A., Christensen, T. A., Salisbury, J. L., & Baack, M. L. (2025) · Cells · doi:10.3390/cells14211698
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Vinothkumar, P., Lin, P.-Y., Cheng, L.-T., Yu, C.-H. A., Hsu, P., Chou, Y., & Hwang‐Verslues, W. W. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.05.686880
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Mahadeo, A., Bammler, T. K., MacDonald, J. W., Zheng, A. R., Yeung, C. K., Himmelfarb, J., & Kelly, E. J. (2025) · Toxicology Reports · doi:10.1016/j.toxrep.2025.102169
“Mitochondrial fusion and fission are finely-tuned processes that are tightly regulated to balance ATP production efficiency with reactive oxygen species production [42].”
Sew, W. Q. G., Molano-Fernández, M., Li, Z., Lange, A., de Ciriza, N. P., Rasmussen, L. J., & Herranz, H. (2025) · PLoS Biology · doi:10.1371/journal.pbio.3003523
“Mitochondrial fusion, by contrast, merges two mitochondria into one, allowing the exchange of mitochondrial contents and supporting function, especially under cellular stress [6,7].”
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Yang, S., Park, H., Ha, H.-W., & Koo, D. (2016) · Journal of Animal Reproduciton and Biotechnology · doi:10.12750/jarb.40.4.207
Jiang, J., Ding, Y., & Wang, F. (2026) · The FASEB Journal · doi:10.1096/fj.202503717r
Kmail, M., Kumar, J., Lin, T. S., & Mohamed, W. (2026) · Research Square · doi:10.21203/rs.3.rs-8426422/v1
Fang, J., Ren, Q., Liu, Y., Danzeng, C., Qiang, W., Wu, B., Zhu, H., & Shang, L. (2026) · Research Square · doi:10.21203/rs.3.rs-8426076/v1
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Kwon, K.-C., & Jang, Y. (2026) · Exercise Science · doi:10.15857/ksep.2025.00626
“Mitochondrial fusion plays a critical role in restoring damaged mitochondria and maintaining intracellular energy homeostasis, with MFN1 and OPA1 serving as key regulatory proteins in this process [17].”
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Sehgal, A., Kumar, P., & Singh, A. (2026) · Probecell Science · doi:10.65807/prob.sci.2025.2.2.5
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“These activities, are closely linked to cellular nutrient levels, stress responses, and aging 2,3 .”
Zhang, Z., Liu, J., & Liu, Q.-J. (2026) · International Journal of Radiation Biology · doi:10.1080/09553002.2026.2630995
“Mitochondrial fusion and fission processes are tightly regulated by a set of highly conserved dynein superfamilies known as large GTPases (Meyer et al. 2017; Adebayo et al. 2021).”
Cai, H., & He, J. (2026) · Oncogenesis · doi:10.1038/s41389-026-00609-1
“Mitochondria are highly dynamic, maternally inherited cytoplasmic organelles that play essential roles in cellular oxidative phosphorylation, metabolic regulation, and calcium homeostasis [5].”
Toledano, J. M., Puche-Juárez, M., Badillo, M. P. C., Díaz‐Castro, J., Sánchez‐Romero, J., Ocaña-Peinado, F. M., Matallana, C. D. P., Martín‐Álvarez, E., Moreno‐Fernández, J., & Ochoa, J. J. (2026) · Life Sciences · doi:10.1016/j.lfs.2026.124338
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“18 These mitochondrial abnormalities are frequently observed in TNBC and correlate with poor clinical outcomes.”
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“These processes are tightly regulated by proteins such as dynamin-related protein 1 (DRP1; fission), and MFN1/2 and optic atrophy 1 (OPA1; fusion), and epigenetic modifications can modulate the expression of these genes in response to environmental stressors [16].”
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“40,59 Thus, enhanced mitochondrial fusion in response to IL-13 is consistent with our finding of diminished ATP level as well as limited respiration and glycolysis in IL-13-treated esophageal keratinocytes.”
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Poinsignon, L. (2024) · theses.fr (ABES) · doi:10.70675/e7ecd618zd48dz4c7aza3afz3459ba1a93c8
Qian, R., Hou, J., Guo, H., Zhang, Q., Lin, J., Zhou, Y., ZhiQiang, B., Shen, J., Yang, X., Wang, S., et al. (2026) · Journal of Materials Chemistry B · doi:10.1039/d5tb02428e
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“55] Mitochondrial fusion and fission are dynamically coordinated processes that influence mitochondrial morphology from fragmented to highly interconnected networks.”
Stavros, S., Christopoulos, P., Dafopoulos, S., Christodoulaki, C., Moustakli, E., Potiris, A., Tzeli, M., Zikopoulos, A., Dafopoulos, K. C., & Drakakis, P. (2026) · Biology · doi:10.3390/biology15131000
“These processes are fundamental for the degradation of dysfunctional mitochondria and for adjusting their activity to metabolic conditions [52,53].”
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“…reduction in MFN2 protein abundance despite preserved transcript levels challenges the interpretation of a uniformly fusion-dominant phenotype and instead supports the possibility that mitochondrial network remodeling is selectively recalibrated rather than globally shifted (Adebayo et al., 2021).”
Athar, F., Houston, E. J., Jewett, E., May, C. K., Duque, M. C., & Templeman, N. M. (2026) · Communications Biology · doi:10.1038/s42003-026-10564-7
“High glucoseinducesmitochondrialdysfunctionin C.elegans bodywallmuscle 24 , thus we examined the morphology of oocyte mitochondrial networks. fi ssion and fusion 41,42 , with elongated mitochondria associated with increased fusion 43 fi ssion.”
ZHANG, Y., Zhu, F., Xiaotian, W. U., Zhansong, L. I., Huang, P., Gao, Y., & Zeng, L. (2026) · Journal of Zhejiang University (Medical Sciences) · doi:10.3724/zdxbyxb-2025-0706
Mitochondrial Dysfunction as a Central Mechanism in Neurodegenerative Disorders
Jain, R. (2026) · Journal of Medical Excellence · doi:10.4103/jome.jome_25_25
Mubeen, M., Arshad, K., Sarfraz, M., Ahmed, F., Khalil, E. R., & Kumar, K. (2026) · Journal of Cardio-oncology · doi:10.1097/co9.0000000000000023
Li, W., Qu, Q., Liu, X., 徐, 国., Shao, G., Ma, B., Jun, L., Hao, X., & Qi, R. (2026) · Cell Death and Disease · doi:10.1038/s41419-026-09080-7
“Mitochondria, which are dynamic organelles that govern energy production and apoptosis, maintain homeostasis through fusion – fi ssion balance, mitophagy, and biogenesis [6 – 10].”
Wu, Q., Fan, D., Ren, J., Xing, Y., Chen, Z., Jin, H., Lu, Y., Wang, X. R., & Zheng, H. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06050-0
“…fusion and fission balance, also known as mitochondrial dynamics, is a pivotal process in MQC that allows cells to meet their metabolic demands, ensures the clearance of damaged organelles, and promotes self-renewal of mitochondria with minimal energetic and resource expenditure [49, 50].”
Saatci, Ö., Ulukan, B., Çetįn, M., Kuasne, H., Martinez, C., Perçin, E., Oleinik, N., Savoca, M. T., Nehme, A., Hernández-Corchado, A., et al. (2026) · Cell Reports Medicine · doi:10.1016/j.xcrm.2026.103015
“13 Mitochondrial fusion enhances mitochondrial integrity and is mediated by mitofusins 1 and 2 (MFN1/2) 14 and OPA1, 15 which coordinate outer and inner membrane fusion, respectively, to ensure efficient ATP production.”
Metabolic regulation and diabetic cardiomyopathy
Du, H., & Chen, C. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-34186-1.00019-0
Han, Y., Ma, L., & Ma, X. (2026) · Biology Direct · doi:10.1186/s13062-026-00908-y
“During this process, mitochondrial dynamics play a central role in maintaining energy homeostasis [260, 261].”
Wang, J., Wu, Z., Fang, L., Guo, Y., Li, H., & 梁凤鸣 (2026) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2026.107000
Zou, Y., Gong, S., Guo, L., 唐伯儒, & Zhang, J. (2026) · Microbiology and Immunology · doi:10.1111/1348-0421.70082
“For pretreatment, to inhibit Drp1 activity, pORF5‐Hela cells were pretreated with 10 μM Mdivi‐1 [35], a selective Drp1 inhibitor, for 1 h.”
Disrupted Mitochondrial Quality Control in Atherosclerotic Disease
Wilcox, T., Hansen, J. A., Blanker, A., & Widlansky, M. E. (2026) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2026.101625
NDUFV2P1-driven modulation of mitochondrial and neuronal activities; implications to schizophreniaPreprint
Lapiro, Y., Karry, R., Binah, O., & Ben‐Shachar, D. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.23.740347
Trujillo-Rangel, W. Á., Escutia-Gutiérrez, R., García‐Benavides, L., Zamudio‐Ojeda, A., Delgado-Lara, D. L. C., García-Mercado, F. G., Padilla-Ponce, D. J., Magallón-Chávez, O., Rivas-Loaiza, J. A., Pérez-Cisneros, M., et al. (2026) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2026.07.005
“Resveratrol is a polyphenolic compound found in grapes and red wine that has been shown to improve mitochondrial fusion and overall mitochondrial (Adebayo et al., 2021)function, in part through the activation of pathways associated with SIRT1 and PGC (cid:0) 1 α (Van der Bliek et al., 2013).”
InfluentialZhao, H., & Chen, M. (2026) · Biology · doi:10.3390/biology15151240
“Mitochondrial fusion enables content exchange between different mitochondria and helps prevent mitochondria degradation, thereby sustaining normal physiological functions [28].”
Metadata
- Authors
- Adebayo, M., Singh, S., Singh, A. P., & Dasgupta, S.
- Affiliations
- USA Mitchell Cancer Institute (US)
- Corresponding author
- Singh, Ajay Pratap
- Dasgupta, Santanu
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2021-05-28
- Volume
- 35
- Issue
- 6
- Pages
- e21620-e21620
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- PMC
- PMC8415099
- OpenAlex
- W3164775823
- Cited by
- 733
- References
- 103
- Citations by year
- 2026: 189 · 2025: 235 · 2024: 183 · 2023: 83 · 2022: 38 · 2021: 4
- FWCI
- 8.11
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (CA185490, CA224306, CA204801, CA231925)
- 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 homeostasis, mitochondrial quality control, mitochondrial division, oxidative phosphorylation, calcium signaling, damage-associated molecular patterns, apoptosis, mitochondrial metabolism, neurodegenerative diseases, cardiovascular disease, cancer
- MeSH terms
- Animals, Homeostasis, Humans, Mitochondria, Mitochondrial Dynamics
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