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, causing endogenous damage-associated molecular patterns production and cytokine release.
“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”
From Inflammation and aging: signaling pathways and intervention therapies (2023) · cites this paper as [203]
The Introduction’s Carcinogenesis section says HMGB1 is released following cell death, injury, or stress, which supports the release of an endogenous damage signal. It does not connect oxidative stress to DAMP production or report the claimed cytokine release; the oxidative-damage clause is separately cited to reference 201. (LLM, conf=0.76)
Experimental — accuracy not yet measuredCytokines activate downstream signaling pathways of pattern recognition receptors, causing systemic chronic inflammatory responses in the body.
“Cytokines activate downstream signaling pathways of pattern recognition receptors,203 causing systemic chronic inflammatory responses in the body.204”
From Inflammation and aging: signaling pathways and intervention therapies (2023) · cites this paper as [203]
Citation 204 is attached to the claim about systemic chronic inflammatory responses. The Introduction > Carcinogenesis discusses HMGB1–RAGE signaling in tumors, and Introduction > Atherosclerosis describes a chronic vascular disease, but neither passage says that cytokine signaling causes systemic chronic inflammation. Searches for systemic chronic inflammatory responses and pattern-recognition-receptor cytokine signaling found no supporting passage; page numbers were not available in our copy. (LLM, conf=0.74)
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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 3,554 · see citing works
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Functions and dysfunctions of mitochondrial dynamics
Detmer, S. A., & Chan, D. C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2275 · Cited by 1,369 · see citing works
PINK1-Phosphorylated Mitofusin 2 Is a Parkin Receptor for Culling Damaged Mitochondria
Chen, Y., & Dorn, G. W. (2013) · Science · doi:10.1126/science.1231031 · Cited by 1,323 · see citing works
Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission.
Taguchi, N., Ishihara, N., Jofuku, A., Oka, T., & Mihara, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607279200 · Cited by 1,226 · see citing works
Fusion and fission: interlinked processes critical for mitochondrial health
Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196 · see citing works
Rambold, A. S., Kostelecky, B., Elia, N., & Lippincott‐Schwartz, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107402108 · Cited by 1,144 · see citing works
Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808249105 · Cited by 1,129 · see citing works
S-Nitrosylation of Drp1 Mediates β-Amyloid-Related Mitochondrial Fission and Neuronal Injury
Cho, D.-H., Nakamura, T., Fang, J., Cieplak, P., Godzik, A., Gu, Z., & Lipton, S. A. (2009) · Science · doi:10.1126/science.1171091 · Cited by 1,092 · see citing works
Cribbs, J. T., & Strack, S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7401062 · Cited by 1,024 · see citing works
Mitochondrial Fusion and Fission in Mammals
Chan, D. C. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104638 · Cited by 972 · see citing works
Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
Ishihara, N., Fujita, Y., Oka, T., & Mihara, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601184 · Cited by 899 · see citing works
Song, Z., Chen, H., Fiket, M., Alexander, C., & Chan, D. C. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704110 · Cited by 818 · see citing works
An Actin-Dependent Step in Mitochondrial Fission Mediated by the ER-Associated Formin INF2
Korobova, F., Ramabhadran, V., & Higgs, H. N. (2013) · Science · doi:10.1126/science.1228360 · Cited by 817 · see citing works
SLP‐2 is required for stress‐induced mitochondrial hyperfusion
Tondera, D., Grandemange, S., Jourdain, A. A., Karbowski, M., Mattenberger, Y., Herzig, S., Cruz, S. D., Clerc, P., Lauria, I., Merkwirth, C., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.89 · Cited by 767 · see citing works
Mitochondrial dynamics regulates migration and invasion of breast cancer cells
Zhao, J., Zhang, J., Yu, M., Xie, Y., Huang, Y., Wolff, D. W., Abel, P. W., & Tu, Y. (2012) · Oncogene · doi:10.1038/onc.2012.494 · Cited by 763 · see citing works
Erk2 Phosphorylation of Drp1 Promotes Mitochondrial Fission and MAPK-Driven Tumor Growth
Kashatus, J. A., Nascimento, A., Myers, L. J., Sher, A., Byrne, F. L., Hoehn, K. L., Counter, C. M., & Kashatus, D. F. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.002 · Cited by 700 · see citing works
Bioenergetic role of mitochondrial fusion and fission
Westermann, B. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.02.033 · Cited by 687 · see citing works
Endosymbiosis and Eukaryotic Cell Evolution
Archibald, J. M. (2015) · Current Biology · doi:10.1016/j.cub.2015.07.055 · Cited by 654 · see citing works
Mitochondrial dynamics, mitophagy and cardiovascular disease
Vásquez-Trincado, C., García‐Carvajal, I., Pennanen, C., Parra, V., Hill, J. A., Rothermel, B. A., & Lavandero, S. (2015) · The Journal of Physiology · doi:10.1113/jp271301 · Cited by 625 · see citing works
Developmentally Regulated Mitochondrial Fusion Mediated by a Conserved, Novel, Predicted GTPase
Hales, K. G., & Fuller, M. T. (1997) · Cell · doi:10.1016/s0092-8674(00)80319-0 · Cited by 611 · see citing works
Inhibition of mitochondrial fission prevents cell cycle progression in lung cancer
Rehman, J., Zhang, H. J., Tóth, P. T., Zhang, Y., Marsboom, G., Hong, Z., Salgia, R., Husain, A. N., Wietholt, C., & Archer, S. L. (2012) · The FASEB Journal · doi:10.1096/fj.11-196543 · Cited by 594 · see citing works
Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage
Griparić, L., Kanazawa, T., & van der Bliek, A. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704112 · Cited by 467 · see citing works
Davies, V. J., Hollins, A. J., Piechota, M. J., Yip, W., Davies, J. R., White, K. E., Nicols, P. P., Boulton, M. E., & Votruba, M. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm079 · Cited by 449 · see citing works
SIRT3 Deacetylates and Activates OPA1 To Regulate Mitochondrial Dynamics during Stress
Samant, S. A., Zhang, H. J., Hong, Z., Pillai, V. B., Sundaresan, N. R., Wolfgeher, D., Archer, S. L., Chan, D. C., & Gupta, M. P. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01483-13 · Cited by 446 · see citing works
Mitochondrial dysfunction and mitochondrial dynamics-The cancer connection
Srinivasan, S., Guha, M., Kashina, A., & Avadhani, N. G. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.01.004 · Cited by 435 · see citing works
Mitochondrial control by DRP1 in brain tumor initiating cells
Xie, Q., Wu, Q., Horbinski, C., Flavahan, W. A., Yang, K., Zhou, W., Dombrowski, S. M., Huang, Z., Fang, X., Shi, Y., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.3960 · Cited by 415 · see citing works
Molecular basis of selective mitochondrial fusion by heterotypic action between OPA1 and cardiolipin
Ban, T., Ishihara, T., Kohno, H., Saita, S., Ichimura, A., Maenaka, K., Oka, T., Mihara, K., & Ishihara, N. (2017) · Nature Cell Biology · doi:10.1038/ncb3560 · Cited by 410 · see citing works
MFN2 mutation distribution and genotype/phenotype correlation in Charcot-Marie-Tooth type 2
Verhoeven, K. (2006) · Brain · doi:10.1093/brain/awl126 · Cited by 408 · see citing works
Huang, Q., Zhan, L., Cao, H., Li, J., Lyu, Y., Guo, X., Zhang, J., Ji, L., Ren, T., An, J., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1166318 · Cited by 392 · see citing works
Parkin Ubiquitinates Drp1 for Proteasome-dependent Degradation
Wang, H., Song, P., Du, L., Tian, W., Yue, W., Liu, M., Li, D., Wang, B., Zhu, Y., Cao, C., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.144238 · Cited by 376 · see citing works
Wang, Q., Zhang, M., Torres, G., Wu, S., Ouyang, C., Xie, Z., & Zou, M.-H. (2017) · Diabetes · doi:10.2337/db16-0915 · Cited by 370 · see citing works
Mitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity
Bertholet, A. M., Delerue, T., Millet, A. M., Moulis, M. F., David, C., Daloyau, M., Arnauné-Pelloquin, L., Davezac, N., Mils, V., Miquel, M. C., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.011 · Cited by 363 · see citing works
Chakrabarti, R., Ji, W.-K., Stan, R. V., de Juan Sanz, J., Ryan, T. A., & Higgs, H. N. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201709111 · Cited by 349 · see citing works
Manor, U., Bartholomew, S. R., Golani, G., Christenson, E. T., Kozlov, M. M., Higgs, H. N., Spudich, J. A., & Lippincott‐Schwartz, J. (2015) · eLife · doi:10.7554/elife.08828 · Cited by 341 · see citing works
Leboucher, G. P., Tsai, Y. C., Yang, M., Shaw, K. C., Zhou, M., Veenstra, T. D., Glickman, M. H., & Weissman, A. M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.041 · Cited by 334 · see citing works
MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion
Cao, Y.-L., Meng, S., Chen, Y., Feng, J.-X., Gu, D.-D., Yu, B., Li, Y.-J., Yang, J.-Y., Liao, S., Chan, D. C., et al. (2017) · Nature · doi:10.1038/nature21077 · Cited by 326 · see citing works
MAPL SUMOylation of Drp1 Stabilizes an ER/Mitochondrial Platform Required for Cell Death
Prudent, J., Zunino, R., Sugiura, A., Mattie, S., Shore, G. C., & McBride, H. M. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.001 · Cited by 321 · see citing works
Lenaers, G., Hamel, C., Delettre, C., Amati‐Bonneau, P., Procaccio, V., Bonneau, D., Reynier, P., & Miléa, D. (2012) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-7-46 · Cited by 299 · see citing works
Abnormal Mitochondrial Morphology in Sporadic Parkinson's and Alzheimer's Disease Cybrid Cell Lines
Trimmer, P. A., Swerdlow, R. H., Parks, J. K., Keeney, P. M., Bennett, J. P., Miller, S. W., Davis, R. E., & Parker, W. D. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7333 · Cited by 296 · see citing works
Abnormal mitochondrial dynamics and neurodegenerative diseases
Su, B., Wang, X., Zheng, L., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.013 · Cited by 289 · see citing works
Mgm1p, a Dynamin-related GTPase, Is Essential for Fusion of the Mitochondrial Outer Membrane
Sesaki, H., Southard, S. M., Yaffe, M. P., & Jensen, R. E. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-12-0788 · Cited by 274 · see citing works
Recent advances into the understanding of mitochondrial fission
Elgass, K., Pakay, J. L., Ryan, M. T., & Palmer, C. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.002 · Cited by 262 · see citing works
Kamerkar, S. C., Kraus, F., Sharpe, A. J., Pucadyil, T. J., & Ryan, M. T. (2018) · Nature Communications · doi:10.1038/s41467-018-07543-w · Cited by 247 · see citing works
Pyakurel, A., Savoia, C., Hess, D., & Scorrano, L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.021 · Cited by 244 · see citing works
Kang, R., Tang, D., Schapiro, N. E., Loux, T., Livesey, K. M., Billiar, T. R., Wang, H., Houten, B. V., Lotze, M. T., & Zeh, H. J. (2013) · Oncogene · doi:10.1038/onc.2012.631 · Cited by 230 · see citing works
Olichon, A., Elachouri, G., Baricault, L., Delettre, C., Belenguer, P., & Lenaers, G. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402048 · Cited by 228 · see citing works
Ban, T., Heymann, J. A. W., Song, Z., Hinshaw, J. E., & Chan, D. C. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq088 · Cited by 222 · see citing works
MFN2 mutations cause severe phenotypes in most patients with CMT2A
Feely, S. M. E., Laurá, M., Siskind, C. E., Sottile, S. L., Davis, M. B., Gibbons, V. S., Reilly, M. M., & Shy, M. E. (2011) · Neurology · doi:10.1212/wnl.0b013e31821a441e · Cited by 217 · see citing works
Li, S., Xu, S., Roelofs, B. A., Boyman, L., Lederer, W. J., Sesaki, H., & Karbowski, M. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201404050 · Cited by 210 · see citing works
Gawlowski, T., Suárez, J., Scott, B. T., Torres‐Gonzalez, M., Wang, H., Schwappacher, R., Han, X., Yates, J. R., Hoshijima, M., & DILLMANN, W. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.390682 · Cited by 204 · see citing works
Givvimani, S., Munjal, C., Tyagi, N., Sen, U., Metreveli, N. S., & Tyagi, S. C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032388 · Cited by 203 · see citing works
Zhang, Z., Li, T., Chen, M., Xu, D., Zhu, Y., Hu, B., Lin, Z., Pan, J.-J., Wang, X., Wu, C., et al. (2019) · British Journal of Cancer · doi:10.1038/s41416-019-0658-4 · Cited by 198 · see citing works
Liang, C., Wang, T. T., Luby‐Phelps, K., & German, D. C. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2006.08.015 · Cited by 186 · see citing works
Clinical and electrophysiologic features of CMT2A with mutations in the mitofusin 2 gene
Lawson, V. H., Graham, B. V., & Flanigan, K. M. (2005) · Neurology · doi:10.1212/01.wnl.0000168898.76071.70 · Cited by 183 · see citing works
Structures of human mitofusin 1 provide insight into mitochondrial tethering
Qi, Y., Yan, L., Yu, C., Guo, X., Zhou, X., Hu, X., Huang, X., Rao, Z., Lou, Z., & Hu, J. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201609019 · Cited by 180 · see citing works
Two Forms of Opa1 Cooperate to Complete Fusion of the Mitochondrial Inner-Membrane
Ge, Y., Shi, X., Boopathy, S., McDonald, J., Smith, A. W., & Chao, L. H. (2020) · eLife · doi:10.7554/elife.50973 · Cited by 174 · see citing works
Mitochondrial fusion exploits a therapeutic vulnerability of pancreatic cancer
Yu, M., Nguyen, N. D., Huang, Y., Lin, D., Fujimoto, T. N., Molkentine, J. M., Deorukhkar, A., Kang, Y., Lucas, F. A. S., Fernandes, C. J., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.126915 · Cited by 173 · see citing works
Salabei, J. K., & Hill, B. G. (2013) · Redox Biology · doi:10.1016/j.redox.2013.10.011 · Cited by 169 · see citing works
The C. elegans Opa1 Homologue EAT-3 Is Essential for Resistance to Free Radicals
Kanazawa, T., Zappaterra, M., Hasegawa, A., Wright, A. P., Newman-Smith, E. D., BUTTLE, K. F., McDonald, K. L., Mannella, C. A., & van der Bliek, A. M. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000022 · Cited by 164 · see citing works
A dimeric equilibrium intermediate nucleates Drp1 reassembly on mitochondrial membranes for fission
Macdonald, P. J., Stepanyants, N., Mehrotra, N., Mears, J. A., Qi, X., Sesaki, H., & Ramachandran, R. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-02-0728 · Cited by 163 · see citing works
Specific Interaction with Cardiolipin Triggers Functional Activation of Dynamin-Related Protein 1
Bustillo-Zabalbeitia, I., Montessuit, S., Raemy, E., Basañez, G., Terrones, O., & Martinou, J.-C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102738 · Cited by 162 · see citing works
Mattie, S., Riemer, J., Wideman, J. G., & McBride, H. M. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201611194 · Cited by 158 · see citing works
Huang, C.-Y., Chiang, S., Chen, W. T., Ke, T., Chen, T.-W., You, Y., Lin, C., Chao, K. S. C., & Huang, C. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1019-6 · Cited by 155 · see citing works
Detmer, S. A., Velde, C. V., Cleveland, D. W., & Chan, D. C. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm314 · Cited by 148 · see citing works
Involvement of Drp1 in hypoxia-induced migration of human glioblastoma U251 cells
Wan, Y., Zhang, J., Yang, Z., Jiang, L., WEI, Y.-F., Lai, Q., WANG, J.-B., XIN, H.-B., & Han, X. (2014) · Oncology Reports · doi:10.3892/or.2014.3235 · Cited by 140 · see citing works
MFN2-related neuropathies: Clinical features, molecular pathogenesis and therapeutic perspectives
Stuppia, G., Rizzo, F., Riboldi, G. M., Bo, R. D., Nizzardo, M., Simone, C., Comi, G. P., Bresolin, N., & Corti, S. P. (2015) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2015.05.033 · Cited by 138 · see citing works
High frequency of mitochondrial complex I mutations in Parkinson’s disease and aging
Smigrodzki, R. M., Parks, J. K., & Parker, W. D. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.020 · Cited by 138 · see citing works
Lee, J., Kapur, M., Li, M., Choi, M., Choi, S., Kim, H.-J., Kim, I., Lee, E. J., Taylor, J. P., & Yao, T. (2014) · Journal of Cell Science · doi:10.1242/jcs.157321 · Cited by 132 · see citing works
Charcot-Marie-Tooth Disease Type 2A
Bombelli, F., Stojkovic, T., Dubourg, O., Echaniz‐Laguna, A., Tardieu, S., Larcher, K., Amati‐Bonneau, P., Latour, P., Vignal, O., Cazeneuve, C., et al. (2014) · JAMA Neurology · doi:10.1001/jamaneurol.2014.629 · Cited by 132 · see citing works
Mitochondrial dynamics and cancer
Maycotte, P., Marín‐Hernández, Á., Goyri-Aguirre, M., Anaya-Ruı́z, M., Reyes‐Leyva, J., & Cortés-Hernández, P. (2017) · Tumor Biology · doi:10.1177/1010428317698391 · Cited by 123 · see citing works
Mitochondrial Fusion Via OPA1 and MFN1 Supports Liver Tumor Cell Metabolism and Growth
Li, M., Wang, L., Wang, Y., Zhang, S., Zhou, G., Lieshout, R., Ma, B., Liu, J., Qu, C., Verstegen, M. M. A., et al. (2020) · Cells · doi:10.3390/cells9010121 · Cited by 123 · see citing works
Expression of mitofusin 2R94Q in a transgenic mouse leads to Charcot–Marie–Tooth neuropathy type 2A
Cartoni, R., Arnaud, E., Médard, J., Poirot, O., Courvoisier, D. S., Chrast, R., & Martinou, J. (2010) · Brain · doi:10.1093/brain/awq082 · Cited by 114 · see citing works
The Impact of Mitochondrial Fusion and Fission Modulation in Sporadic Parkinson’s Disease
Santos, D., Esteves, A. R., Silva, D. F., Januário, C., & Cardoso, S. M. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8893-4 · Cited by 111 · see citing works
The rescue of microtubule-dependent traffic recovers mitochondrial function in Parkinson's disease
Esteves, A. R., Gozes, I., & Cardoso, S. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.10.003 · Cited by 107 · see citing works
Reddy, P. H. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.03.020 · Cited by 106 · see citing works
OPA1 cleavage depends on decreased mitochondrial ATP level and bivalent metals
Baricault, L., Ségui, B., Guégand, L., Olichon, A., Valette, A., Larminat, F., & Lenaers, G. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.08.008 · Cited by 103 · see citing works
White, K., Davies, V. J., Hogan, V. E., Piechota, M. J., Nichols, P. P., Turnbull, D. M., & Votruba, M. (2009) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.08-2913 · Cited by 98 · see citing works
The role of mitochondrial dynamics in human cancers.
Ma, Y., Wang, L., & Jia, R. (2020) · PubMed Central · Cited by 98 · see citing works
Javadov, S. A., Rajapurohitam, V., Kilić, A., Hunter, J. C., Zeidan, A., Faruq, N. S., Escobales, N., & Karmazyn, M. (2010) · Basic Research in Cardiology · doi:10.1007/s00395-010-0122-3 · Cited by 92 · see citing works
Chen, L., Zhang, J., Lyu, Z., Chen, Y., Ji, X., Cao, H., Jin, M., Zhu, J., Jin, Y., Ling, R., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1083-y · Cited by 84 · see citing works
Cofilin1-dependent actin dynamics control DRP1-mediated mitochondrial fission
Rehklau, K., Hoffmann, L., Gurniak, C. B., Ott, M., Witke, W., Scorrano, L., Culmsee, C., & Rust, M. B. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.448 · Cited by 83 · see citing works
Arduíno, D. M., Esteves, A. R., Cortes, L., Silva, D. F., Patel, B., Grazina, M. M., Swerdlow, R. H., Oliveira, C. R., & Cardoso, S. M. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds309 · Cited by 82 · see citing works
Enhanced mitochondrial fission suppresses signaling and metastasis in triple-negative breast cancer
Humphries, B. A., Cutter, A. C., Buschhaus, J. M., Chen, Y., Qyli, T., Palagama, D. S. W., Eckley, S. S., Robison, T. H., Bevoor, A. S., Chiang, B., et al. (2020) · Breast Cancer Research · doi:10.1186/s13058-020-01301-x · Cited by 81 · see citing works
Microtubule depolymerization potentiates alpha-synuclein oligomerization
Esteves, A. R. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/neuro.24.005.2009 · Cited by 71 · see citing works
Cheng, C.-T., Kuo, C., Ouyang, C., Li, C., Chung, Y., Chan, D. C., Kung, H.-J., & Ann, D. K. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2921 · Cited by 66 · see citing works
Arduíno, D. M., Esteves, A. R., & Cardoso, S. M. (2011) · Parkinson s Disease · doi:10.4061/2011/767230 · Cited by 59 · see citing works
Machiela, E., Liontis, T., Dues, D. J., Rudich, P. D., Traa, A., Wyman, L., Kaufman, C., Cooper, J. F., Lew, L., Nadarajan, S., et al. (2020) · The FASEB Journal · doi:10.1096/fj.201903235r · Cited by 59 · see citing works
The role of dynamin-related protein 1 in cancer growth: a promising therapeutic target?
Qian, W., Wang, J., & Houten, B. V. (2013) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.823160 · Cited by 57 · see citing works
Improved Locus-Specific Database forOPA1Mutations Allows Inclusion of Advanced Clinical Data
Ferré, M., Caignard, A., Miléa, D., Leruez, S., Cassereau, J., Chevrollier, A., Amati‐Bonneau, P., Verny, C., Bonneau, D., Procaccio, V., et al. (2014) · Human Mutation · doi:10.1002/humu.22703 · Cited by 54 · see citing works
Mitochondrial Reprogramming Regulates Breast Cancer Progression
Kannan, A., Wells, R. B., Sivakumar, S., Komatsu, S., Singh, K. P., Samten, B., Philley, J. V., Sauter, E. R., Ikebe, M., Idell, S., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-2456 · Cited by 53 · see citing works
Self-citationBannerman, P. G. C., Burns, T., Xu, J., Miers, L. A., & Pleasure, D. (2016) · PLoS ONE · doi:10.1371/journal.pone.0167573 · Cited by 39 · see citing works
Mitochondrial fission and fusion
Patrushev, M. V., Mazunin, I., Vinogradova, E. N., & Kamenski, P. A. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915110061 · Cited by 29 · see citing works
Ropivacaine Prevents the Activation of the NLRP3 Inflammasome Caused by High Glucose in HUVECs
Huang, X., Jiang, J., Huang, L., Ren, Q., Gao, X., & Yu, S. (2020) · ACS Omega · doi:10.1021/acsomega.0c03143 · Cited by 3 · see citing works
Bannerman, P. G. C., Burns, T., Xu, J., Miers, L. A., & Pleasure, D. (2018) · PLoS ONE · doi:10.1371/journal.pone.0204536 · Cited by 1 · see citing works
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Inflammation and aging: signaling pathways and intervention therapies
Li, X., Li, C., Zhang, W., Wang, Y., Qian, P., & Huang, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01502-8 · Cited by 1,443 · see citing works
“Oxidative stress leads to oxidative damage to biomolecules (especially DNA),(201) causing endogenous damageassociated molecular patterns (DAMPs) production and cytokine release in the organism.(202,203) Cytokines activate downstream signaling pathways of pattern recognition receptors,(203) causing systemic chronic inf…”
BackgroundMitochondria: It is all about energy
Casanova, A., Wevers, A., Ledesma, S. N., & Pruimboom, L. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1114231 · Cited by 335 · see citing works
Pang, B., Dong, G., Pang, T., Sun, X., Liu, X., Nie, Y., & Chang, X. (2024) · Angiogenesis · doi:10.1007/s10456-024-09938-4 · Cited by 276 · see citing works
Mitochondrial Glutathione in Cellular Redox Homeostasis and Disease Manifestation
Chen, T., Wang, H., Chang, C.-J., & Lee, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25021314 · Cited by 241 · see citing works
“Unlike mitochondrial fission, which promotes apoptosis, mitochondrial fusion occurs via the interferon-responsive cGAMP interactor 1–mitochondrial fusion 1/2 (MFN1/2) pathway [116].”
BackgroundHong, X., Isern, J., Campanario, S., Perdiguero, E., Ramírez-Pardo, I., Segalés, J., Hernansanz-Agustín, P., Curtabbi, A., Deryagin, O., Pollán, A., et al. (2022) · Cell stem cell · doi:10.1016/j.stem.2022.07.009 · Cited by 213 · see citing works
Chaudhary, M. R., Chaudhary, S., Sharma, Y., Singh, T. A., Mishra, A. K., Sharma, S. G., & Mehdi, M. M. (2023) · Biogerontology · doi:10.1007/s10522-023-10050-1 · Cited by 210 · see citing works
Mitochondrial quality control in human health and disease
Liu, B., Xu, C.-Z., Liu, Y., Lu, Z., Fu, T.-L., Li, G., Deng, Y., Luo, G., Ding, S. Z., Li, N., et al. (2024) · Military Medical Research · doi:10.1186/s40779-024-00536-5 · Cited by 189 · see citing works
Yi, L., Shang, X., Lv, L., Wang, Y., Zhang, J., Quan, C., Shi, Y., Liu, Y., & Zhang, L. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05364-w · Cited by 131 · see citing works
“Mitochondrial dynamics is associated with various cellular processes, including mitochondrial quality control, metabolic adaptation, regulation of mitophagy and apoptosis [18].”
BackgroundInfluentialThe role of mitochondrial dynamics in cerebral ischemia-reperfusion injury
Huang, J., Chen, L., Yao, Z., Sun, X., Tong, X., & Dong, S. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114671 · Cited by 128 · see citing works
The Balance of MFN2 and OPA1 in Mitochondrial Dynamics, Cellular Homeostasis, and Disease
Zanfardino, P., Amati, A., Perrone, M., & Petruzzella, V. (2025) · Biomolecules · doi:10.3390/biom15030433 · Cited by 125 · see citing works
“These mechanisms enable the mitochondrial network to adapt to challenges such as protein misfolding, oxidative stress, and organelle damage [68,69].”
Zhang, X., Zhou, H., & Chang, X. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03599-w · Cited by 114 · see citing works
“Mitochondrial fusion is involved in the communication of genetic material and metabolic substrates among different mitochondria, thereby maintaining mitochondrial stability and integrity (Adebayo et al. 2021).”
BackgroundMolecular Pathophysiological Mechanisms in Huntington’s Disease
Jurcău, A. (2022) · Biomedicines · doi:10.3390/biomedicines10061432 · Cited by 111 · see citing works
Regulation of the NLRP3 inflammasome by autophagy and mitophagy
Gupta, S., Cassel, S. L., Sutterwala, F. S., & Dagvadorj, J. (2024) · Immunological Reviews · doi:10.1111/imr.13410 · Cited by 112 · see citing works
“112,115 The fusion of the two membranes of the mitochondria are separately regulated; OMM fusion is facilitated by homo-and heterodimers of mitofusins Mfn1 and Mfn2, while the fusion of the IMM is regulated by long and short isomers of optic atrophy gene 1 (OPA1).”
Pokharel, M. D., Flores, A. G., Marciano, D. P., Franco, M. C., Fineman, J. R., Aggarwal, S., Wang, T., & Black, S. M. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103049 · Cited by 113 · see citing works
“The optimal balance of fission and fusion is critical for mitochondrial homeostasis [8 – 12].”
BackgroundLi, Y., Guo, M., Niu, S., Shang, M., Chang, X., Sun, Z., Zhang, R., Shen, X., & Xue, Y. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110502 · Cited by 108 · see citing works
Miller, D. M., McCauley, K. F., & Dunham‐Snary, K. J. (2025) · Endocrinology Diabetes & Metabolism · doi:10.1002/edm2.70132 · Cited by 125 · see citing works
“In MASLD, this balance is disrupted, leading to excessive mitochondrial fragmentation or elongation, impacting their function and contributing to disease progression [75] (Figure 5).”
Mitochondrial dysfunction in chronic neuroinflammatory diseases (Review)
Qin, P., Sun, Y., & Li, L. (2024) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2024.5371 · Cited by 104 · see citing works
Wang, Y., Shi, Y., Shao, Y., Lu, X., Zhang, H., & Miao, C. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06849-6 · Cited by 98 · see citing works
“Speci fi cally, fusion allows mitochondria to transfer gene products for optimal function [13], while fi ssion induces the isolation of impaired mitochondria for degradation through mitophagy (a selective form of autophagy) [14].”
BackgroundLiu, D., Qin, H., Gao, Y., Sun, M., & Wang, M. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107258 · Cited by 92 · see citing works
Sun, Y., Yang, Y.-M., Hu, Y.-Y., Ouyang, L., Sun, Z., Yin, X., Li, N., He, Q., & Wang, Y. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102334 · Cited by 90 · see citing works
“The balance of mitochondrial dynamics is a principal procedure to sustain cellular homeostasis [25].”
BackgroundMitochondrial Dysfunction in Metabolic Dysfunction Fatty Liver Disease (MAFLD)
Zhao, Y., Zhou, Y., Wang, D., Huang, Z., Xiao, X., Zheng, Q., Li, S., Long, D., & Feng, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417514 · Cited by 86 · see citing works
“The imbalance between mitochondrial dynamics is key to determining the total mass of mitochondrial cells in the pathogenesis of MAFLD or MASH models [53–59].”
BackgroundMitochondrial dysfunction at the crossroad of cardiovascular diseases and cancer
Rocca, C., Soda, T., Francesco, E. D. D., Fiorillo, M., Moccia, F., Viglietto, G., Angelone, T., & Amodio, N. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04498-5 · Cited by 82 · see citing works
“Mitofusin 1 and 2 (MFN1/2) and optic atrophy 1 (OPA1) are responsible for fusion, while dynamin-related protein 1 (DRP1) and dynamin-2 (DNM2) are the primary fission proteins [32–34].”
BackgroundYan, Y., Li, M., Lin, J., Ji, Y., Wang, K., Yan, D., Shen, Y., Wang, W., Huang, Z., Jiang, H., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.947387 · Cited by 81 · see citing works
“Fission is necessary for the creation of new mitochondria, it provides the raw material for new mitochondria and also contributes to quality control by the removal of damaged mitochondria and facilitates apoptosis (Adebayo et al., 2021).”
BackgroundKhatun, J., Gelles, J. D., & Chipuk, J. E. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.09.004 · Cited by 75 · see citing works
Role of mitochondria in physiological activities, diseases, and therapy
Wang, L., Zhou, X., & Lu, T. (2025) · Molecular Biomedicine · doi:10.1186/s43556-025-00284-5 · Cited by 79 · see citing works
“1a) [49].”
The role of mitochondrial dysfunction in periodontitis: From mechanisms to therapeutic strategy
Jiang, W., Wang, Y., Cao, Z., Chen, Y., Si, C., Sun, X., & Huang, S. (2023) · Journal of Periodontal Research · doi:10.1111/jre.13152 · Cited by 70 · see citing works
Ferroptosis triggers mitochondrial fragmentation via Drp1 activation
Pedrera, L., Clemente, L. P., Dahlhaus, A., Nasudivar, S. L., Tishina, S., González, D. O., Stroh, J., Yapici, F. I., Singh, R. P., Grotehans, N., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-024-07312-2 · Cited by 70 · see citing works
Yu, T., Wang, L., Zhang, L., & Deuster, P. A. (2023) · Antioxidants · doi:10.3390/antiox12061163 · Cited by 71 · see citing works
“The molecular mechanisms of mitochondrial fusion have been reviewed extensively elsewhere [56,60,63,64].”
BackgroundMitochondria-targeted fluorophore: State of the art and future trends
Ding, Q., Wang, X., Luo, Y., Leng, X., Li, X., Gu, M., & Kim, J. S. (2024) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2024.215772 · Cited by 68 · see citing works
Palabıyık, A. A., & Palabıyık, E. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-10368-8 · Cited by 70 · see citing works
“5 [31].”
Jurcău, A., & Jurcău, M. C. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.360289 · Cited by 67 · see citing works
“In depolarized mitochondria, PINK1 stabilizes at the OMM and is no longer imported to the IMM, favouring mitochondrial Parkin translocation (Kazlauskaite et al., 2015).”
BackgroundInfluentialMitochondrial dysfunction in Alzheimer's disease: Guiding the path to targeted therapies
Percy, K. C. M., Liu, Z., & Qi, X. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2025.e00525 · Cited by 67 · see citing works
Mitochondrial cristae in health and disease
Huang, C., Deng, K., & Wu, M. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.123755 · Cited by 63 · see citing works
Peng, Y., Zhao, L., Hu, K., Yang, Y., Ma, J., Zhai, Y., Jiang, Y., & Zhang, D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810920 · Cited by 61 · see citing works
Role of eIF5A in Mitochondrial Function
Barba‐Aliaga, M., & Alepuz, P. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031284 · Cited by 60 · see citing works
Gu, Y., Zhao, X., Zhang, N., Yang, Y., Yi, Y., Shao, Q.-H., Liu, M.-X., & Zhang, X.-L. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102577 · Cited by 58 · see citing works
The Role of Mitochondria Dysfunction in Inflammatory Bowel Diseases and Colorectal Cancer
Kłos, P., & Dabravolski, S. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111673 · Cited by 57 · see citing works
“Further damaged mitochondria are delivered to lysosomes for disposal, while healthy parts could reincorporate into the mitochondria network [20].”
BackgroundFerretti, G. D. S., Quaas, C. E., Bertolini, I., Zuccotti, A., Saatci, Ö., Kashatus, J. A., Sharmin, S., Lu, D. Y., Poli, A. N. R., Quesnelle, A. F., et al. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01310-9 · Cited by 57 · see citing works
“We found that treatment of mice with AP-4-139B led to a signi fi cant decrease in metastatic potential; this was accompanied by a decrease in lung weights and a decrease in Ki67 staining, a marker of proliferation, in lung metastases of mice treated with AP-4-139B (Fig.”
BackgroundMitochondrial Quality Control: A Pathophysiological Mechanism and Therapeutic Target for Stroke
Yang, M., He, Y. T., Deng, S., Xiao, L., Tian, M., Xin, Y., Lu, C., Zhao, F., & Gong, Y. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.786099 · Cited by 56 · see citing works
Effect of Fluoride on Cytotoxicity Involved in Mitochondrial Dysfunction: A Review of Mechanism
Wei, M., Ye, Y., Ali, M. M., Chamba, Y., Tang, J., & Shang, P. (2022) · Frontiers in Veterinary Science · doi:10.3389/fvets.2022.850771 · Cited by 56 · see citing works
“Fluorosis can cause mitochondrial dysfunction, which is partly due to the disruption of the balance betweenmitochondrial fission and fusion, which leads to changes in the morphology of mitochondria, which in turn leads to mitochondrial dysfunction (122).”
BackgroundMTFR2-dependent mitochondrial fission promotes HCC progression
La, Z., Zhang, X., Liu, H., Yang, C., Yu, J., Zhao, W., Guo, J., Zhou, B., & Jiang, N. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-023-04845-6 · Cited by 55 · see citing works
“The maintenance of mitochondrial integrity and homeostasis is crucial and relies on mitochondrial dynamics [5].”
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 60 · see citing works
Lu, L., Liu, J., Wang, J., Lian, C.-Y., Wang, Z., & Wang, L. (2022) · Environmental Pollution · doi:10.1016/j.envpol.2022.120314 · Cited by 53 · see citing works
Tang, S., Fuß, A., Fattahi, Z., & Culmsee, C. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07015-8 · Cited by 53 · see citing works
“…fi ssion process, which is responsible for the subcellular distribution of mitochondria under physiological conditions, for cytochrome C release during apoptosis e.g., in response to oxidative stress, and for mitochondrial quality control through facilitating mitophagy of damaged organelles [5, 6].”
BackgroundReductive stress and mitochondrial dysfunction: The hidden link in chronic disease
Mercola, J. M. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.03.029 · Cited by 52 · see citing works
Mitofusins: from mitochondria to fertility
Zhao, S., Heng, N., Wang, H., Wang, H., Zhang, H., Gong, J., Hu, Z., & Zhu, H. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04386-z · Cited by 53 · see citing works
“It has been established that the impairment of mitochondrial fusion leads to a reduction in glycolysis, OXPHOS, and the Krebs cycle [7, 8].”
BackgroundRecent advances in the pharmacological applications and liver toxicity of triptolide
Cui, D., Xu, D., Yue, S., Yan, C., Liu, W., Fu, R., Ma, W., & Tang, Y. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110651 · Cited by 49 · see citing works
Standpoints in mitochondrial dysfunction: Underlying mechanisms in search of therapeutic strategies
Videla, L. A., Mariman, A. P., Ramos, B., Silva, M. J., & del Campo, A. (2022) · Mitochondrion · doi:10.1016/j.mito.2021.12.006 · Cited by 48 · see citing works
Molecular basis of the morphogenesis of sperm head and tail in mice
Yogo, K. (2022) · Reproductive Medicine and Biology · doi:10.1002/rmb2.12466 · Cited by 47 · see citing works
Liu, X., Ye, M., & Ma, L. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1022821 · Cited by 48 · see citing works
“According to the literature, mitochondrial fusion maintains mitochondrial function by enabling the exchange of contents, whereas excessive mitochondrial fission worsens mitochondrial function and is regarded as an indication of dysfunction (Chen and Chan, 2010; Adebayo et al., 2021).”
BackgroundYe, F., Wu, L., Li, H., Peng, X., Xu, Y., Li, W., Wei, Y., Chen, F., Zhang, J., & Liu, Q. (2023) · Environmental Pollution · doi:10.1016/j.envpol.2023.121084 · Cited by 46 · see citing works
Therapeutic Effects of Mesenchymal Stromal Cells Require Mitochondrial Transfer and Quality Control
Mukkala, A. N., Jerkic, M., Khan, Z., Szaszi, K., Kapus, A., & Rotstein, O. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115788 · Cited by 45 · see citing works
Chen, X., Yang, T., Zhou, Y., Mei, Z., & Zhang, W. (2024) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14725 · Cited by 45 · see citing works
“51 An imbalance in mitochondrial dy - namics results in an alteration of mitochondrial quantity, morphology, and function, leading to CIRI.”
BackgroundZhao, M., Xie, J., Zhang, J., Zhao, B., Zhang, Y., Xue, J., Zhang, R., Zhang, R., Wang, H., Li, Y., et al. (2024) · Environmental Pollution · doi:10.1016/j.envpol.2024.124935 · Cited by 44 · see citing works
Epidemiology, Genetic Etiology, and Intervention of Premature Ovarian Insufficiency
Guo, T., Liu, H., Xu, B., Qi, Y., Xu, K., Wu, X., He, X., Qin, Y., & Chen, Z. (2025) · Endocrine Reviews · doi:10.1210/endrev/bnaf011 · Cited by 44 · see citing works
HIF-1 signaling: an emerging mechanism for mitochondrial dynamics
Xin, Y., Zhao, L., & Peng, R. (2023) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-023-00966-0 · Cited by 43 · see citing works
“Therefore, abnormal mitochondrial dynamics were thought to be a precursor to axonal degradation and eventually resulted in neurodegenerative disorders [1, 6, 24].”
BackgroundAging promotes an increase in mitochondrial fragmentation in astrocytes
Araujo, A. P. B., Vargas, G., Hayashide, L. D. S., Matias, I., Andrade, C. B. V., de Carvalho, J. J., Gomes, F. C. A., & Diniz, L. P. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1496163 · Cited by 43 · see citing works
The role of Mitochondrial Fission Proteins in Mitochondrial Dynamics in Kidney Disease
Qin, L., & Xi, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314725 · Cited by 44 · see citing works
Lysosomes in retinal health and disease
Boya, P., Kaarniranta, K., Handa, J. T., & Sinha, D. (2023) · Trends in Neurosciences · doi:10.1016/j.tins.2023.09.006 · Cited by 43 · see citing works
The role of mitochondrial dynamics in disease
Wang, Y., Dai, X., Li, H., Jiang, H., Zhou, J.-F., Zhang, S., Guo, J., Shen, L., Yang, H., Lin, J. M., et al. (2023) · MedComm · doi:10.1002/mco2.462 · Cited by 40 · see citing works
“8,12,57 For example, mitochondrial with dysfunction fuse with normal mitochondria, mtDNA is reintegrated and renewed, and mitochondrial membrane potential (MMP) returns to normal levels.”
BackgroundResultInfluentialZhao, X., Zhang, J., Li, C., Kuang, W., Deng, J., Tan, X., Li, C., & Li, S. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101975 · Cited by 44 · see citing works
Kobayashi, H., Imanaka, S., Yoshimoto, C., Matsubara, S., & Shigetomi, H. (2024) · Reproductive Medicine and Biology · doi:10.1002/rmb2.12577 · Cited by 41 · see citing works
“41 Mitochondrial fission is crucial for mitochondrial quality control mechanism that eliminates damaged mitochondria via mitophagy.”
BackgroundInfluentialCheung, C., Tu, S., Feng, Y., Wan, C., Ai, H., & Chen, Z. (2024) · Archives of Gerontology and Geriatrics · doi:10.1016/j.archger.2024.105522 · Cited by 43 · see citing works
Fogo, G. M., Raghunayakula, S., Emaus, K. J., Torres, F. J. T., Wider, J. M., & Sanderson, T. H. (2024) · The FASEB Journal · doi:10.1096/fj.202400313r · Cited by 42 · see citing works
Multiple roles of mitochondrial autophagy receptor FUNDC1 in mitochondrial events and kidney disease
Li, K., Xia, X., & Tong, Y. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1453365 · Cited by 41 · see citing works
Huynh, T. V., Rethi, L., Rethi, L., Chen, C., Chen, Y., & Kao, Y. (2023) · Cells · doi:10.3390/cells12091223 · Cited by 40 · see citing works
“Reduction and escalation of any of these dynamic processes due to pathological or physiological stressors results in an imbalance affecting mitochondrial function, ultimately leading to multiple disorders in cardiovascular, neurodegenerative, metabolic diseases, and cancer [20,21].”
BackgroundA Holistic Perspective on Living Aggregate
He, W., Kwok, R. T. K., Qiu, Z., Zhao, Z., & Tang, B. Z. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c09892 · Cited by 40 · see citing works
Recent development of mitochondrial metabolism and dysfunction in osteoarthritis
Guo, P., Alhaskawi, A., Moqbel, S. A. A., & Pan, Z. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1538662 · Cited by 67 · see citing works
Feng, X., Li, C.-Y., Zhang, H., Zhang, P., Shahzad, M., Du, W., & Zhao, X. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094808 · Cited by 39 · see citing works
“Uninterrupted fission and fusion processes in mitochondria are essential for maintaining optimal mitochondrial activity, integrity and internal homeostasis [99].”
BackgroundZhang, X., Wang, L., Li, B., Shi, J., Xu, J. F., & Yuan, M. (2023) · Pharmaceuticals · doi:10.3390/ph16020277 · Cited by 39 · see citing works
Light and electron microscopy continuum-resolution imaging of 3D cell cultures
D’Imprima, E., Montero, M. G., Gawrzak, S., Ronchi, P., Zagoriy, I., Schwab, Y., Jechlinger, M., & Mahamid, J. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.03.001 · Cited by 39 · see citing works
Mitochondrial Dysfunction-Associated Mechanisms in the Development of Chronic Liver Diseases
Arumugam, M. K., Gopal, T., Kandy, R. R. K., Boopathy, L. K., Perumal, S. K., Ganesan, M., Rasineni, K., Donohue, T. M., Osna, N. A., & Kharbanda, K. K. (2023) · Biology · doi:10.3390/biology12101311 · Cited by 38 · see citing works
“Mitochondrial fusion and fission help to maintain organelle homeostasis and allow mitochondrial metabolism to be precisely tuned to cellular needs [177].”
BackgroundLiu, Z., Han, X., You, Y., Xin, G., Li, L., Gao, J., Meng, H., Cao, C., Liu, J., Zhang, Y., et al. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.117690 · Cited by 37 · see citing works
The multifaceted roles of natural products in mitochondrial dysfunction
Chen, Q., Ruan, D., Shi, J., Du, D., & Bian, C. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1093038 · Cited by 36 · see citing works
“material exchange in mitochondria to compensate for mitochondrial function, and mitochondrial fission removes damaged mitochondria through mitophagy (Adebayo et al., 2021).”
BackgroundMitochondrion: A bridge linking aging and degenerative diseases
Zhang, L., Wu, J., Zhu, Z., He, Y., & Fang, R. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121666 · Cited by 38 · see citing works
Riou, M., Enache, I., Sauer, F., Charles, A., & Gény, B. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119572 · Cited by 37 · see citing works
“Indeed, mitochondria can move, fragment (also called fission) or fuse, and mitochondrial division is crucial to maintain the number and distribution of mitochondria in cells and to transfer gene products between mitochondria [54].”
BackgroundLiu, X., Song, L., Yu, J., Huang, F., Li, Y., & Ma, C. (2022) · PubMed · doi:10.14670/hh-18-443 · Cited by 35 · see citing works
Mitochondrial dysfunction in pulmonary arterial hypertension
Zhang, W., Liu, B., Wang, Y., Zhang, H., He, L., Wang, P., & Dong, M. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.1079989 · Cited by 35 · see citing works
“Mitochondrial division is crucial to maintain the number and proper distribution of mitochondria in daughter cells (Adebayo et al., 2021).”
BackgroundMitochondrial Dysfunction in Systemic Lupus Erythematosus with a Focus on Lupus Nephritis
Halfon, M., Tankeu, A. T., & Ribi, C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25116162 · Cited by 36 · see citing works
“This process plays a role in inheritance and mitochondrial partitioning during cell division, apoptosis, and mitophagy [29].”
BackgroundBassiouni, W., y Valencia, R. H., Mahmud, Z., Seubert, J. M., & Schulz, R. (2023) · Basic Research in Cardiology · doi:10.1007/s00395-023-00999-y · Cited by 34 · see citing works
“Mfn-2, as an outer mitochondrial membrane fusion protein, mediates the docking and fusion of mitochondria through the oligomerization of the GTPase domains of different Mfn-2 proteins [1].”
Harnessing Mitophagy for Therapeutic Advances in Aging and Chronic Neurodegenerative Diseases
Ghosh, D., & Kumar, A. (2024) · Neuroglia · doi:10.3390/neuroglia5040026 · Cited by 36 · see citing works
“Fusion is vital for preventing the accumulation of mitochondrial damage and supporting biogenesis [28,29].”
Metabolic and Mitochondrial Dysregulations in Diabetic Cardiac Complications
Tashkandi, A. J. A., Gorman, A., Mathers, E. M., Carney, G., Yacoub, A., Setyaningsih, W. A. W., Kuburas, R., & Margariti, A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26073016 · Cited by 35 · see citing works
“Mitochondria make up roughly 40% of the volume of cardiac cells, which is necessary to keep up with the high demand for cardiac function [203].”
Established and emerging roles for mitochondria in neutrophils
Peng, S., Gao, J., Stojkov, D., Yousefi, S., & Simon, H. (2022) · Immunological Reviews · doi:10.1111/imr.13158 · Cited by 33 · see citing works
Mitochondrial Dysfunction and Metabolic Reprogramming in Obesity and Asthma
Hartsoe, P., Holguín, F., & Chu, H. W. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052944 · Cited by 36 · see citing works
“Fusion is controlled by GTPase proteins Mitofusin 1 (Mfn1), Mitofusin 2 (Mfn2), and Optic atrophy protein (OPA1) [29].”
BackgroundTurkington, R. E., Hukriede, N. A., Ho, J., Jayasundara, N., & Sanders, A. P. (2025) · Environmental Science and Pollution Research · doi:10.1007/s11356-025-36538-6 · Cited by 33 · see citing works
“Processes such as mitochondrial signaling, biogenesis, fission, fusion, and mitophagy are essential to maintaining mitochondrial function and optimal ATP production (Bhargava and Schnellmann 2017, Popov 2020, Adebayo et al. 2021).”
Kong, Y., Akatsuka, S., Motooka, Y., Zheng, H., Cheng, Z., Shiraki, Y., Mashimo, T., Imaoka, T., & Toyokuni, S. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102356 · Cited by 34 · see citing works
“This was also confirmed by a decrease in the protein levels regulating mitochondrial fusion (Mitofusion1/2 and Opa1) and fission (Drp1) [38] in the MUT kidney at 3 weeks of the carcinogenesis protocol (Figs.”
BackgroundZhou, J., Hao, J., Zhong, Z., Yang, J., Lv, T., Zhao, B., Lin, H., Chi, J., & Guo, H. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0355 · Cited by 32 · see citing works
“Mitochondrial fission is also important for maintaining the proper distribution and quantity of mitochondria in daughter cells and is beneficial in situations where large amounts of energy are required (Adebayo et al., 2021).”
Lyu, Y.-T., Huo, J., Jiang, W., Yang, W., Yang, W., Wang, S., Cheng, Y., Jiang, Z., & Shan, Q. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.175531 · Cited by 32 · see citing works
Sultana, M. A., Hia, R. A., Akinsiku, O., & Hegde, V. K. (2023) · Biology · doi:10.3390/biology12071019 · Cited by 31 · see citing works
“A subtle balance between mitochondrial fusion and fission is essential for cell survival and optimal function [48].”
BackgroundFang, X., Xia, W., Li, S., Qi, Y., Liu, M., Yu, Y., Li, H., Li, M., Tao, C., Wang, Z., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23095013 · Cited by 31 · see citing works
“Mitochondria are interconnecting and highly dynamic cellular organelles whose homeostasis requires a stable equilibrium in a multitude of processes including fission, fusion, and biogenesis [24].”
BackgroundMitochondrial Control in Inflammatory Gastrointestinal Diseases
Sui, G.-Y., Wang, F., Lee, J., & Roh, Y. S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314890 · Cited by 30 · see citing works
The Journey of Mitochondrial Protein Import and the Roadmap to Follow
Haastrup, M. O., Vikramdeo, K. S., Singh, S., Singh, A. P., & Dasgupta, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032479 · Cited by 30 · see citing works
“(12S and 16S rRNA), and 22 transfer RNAs [6].”
InfluentialSelf-citationHao, W., Cha, R., Wang, M., Li, J., Guo, H., Du, R., Zhou, F., & Jiang, X. (2023) · ACS Nano · doi:10.1021/acsnano.3c01656 · Cited by 30 · see citing works
New therapeutic directions in type II diabetes and its complications: mitochondrial dynamics
Wang, S., Zhao, H., Lin, S., Lv, Y., Lin, Y. N., Liu, Y., Peng, R., & Jin, H. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1230168 · Cited by 32 · see citing works
“Abbreviations: ROS, reactive oxygen species; OS, oxidative stress; Mfn1, mitofusin-1; Mfn2, mitofusin-2; Opa1, optic atrophy 1; Drp1, dynamin related protein 1; Fis1, mitochondrial fission 1; MFF, mitochondrial fission factor; T2D, type II diabetes; OMM, outer mitochondrial membrane; HR1, helix regions 1; HR2, helix r…”
BackgroundInfluentialGao, J., & Hou, T. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114999 · Cited by 31 · see citing works
Zhou, L., Su, W., Wang, Y., Zhang, Y., Xia, Z., & Lei, S. (2023) · Diabetes Obesity and Metabolism · doi:10.1111/dom.15369 · Cited by 29 · see citing works
“43,44 Fission in mammals is coordinated by a large dynamin-like GTPase, DRP1, which is recruited to the mitochondria by adaptors present on the outer mitochondrial membrane, including MFF, MID49, MID51 and FIS1.”
BackgroundLi, Q., Guo, P., Wang, S., Su, L., Liang, T., Yu, W., Guo, J., Yang, Q., Tang, Z., & Liao, J. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.169642 · Cited by 29 · see citing works
Latino, D., Venditti, M., Falvo, S., Grillo, G., Santillo, A., Messaoudi, I., Rhouma, M. B., Minucci, S., Baccari, G. C., & Fiore, M. M. D. (2024) · Cells · doi:10.3390/cells13060523 · Cited by 29 · see citing works
“In this regard, several proteins are involved in such dynamic activities: Dynamin-associated protein 1 (DRP1) regulates mitochondrial fission, while Mitofusin 1 and 2 (MFN1 and MFN2), dynamin-like GTPases, and the protein optic atrophy 1 (OPA1), are involved in mitochondrial fusion [8].”
BackgroundJeong, I., Cho, E., Yook, J.-S., Choi, Y., Park, D., Kang, J., Lee, S.-H., Seo, D. Y., Jung, S., & Kwak, H. (2024) · Life · doi:10.3390/life14080962 · Cited by 33 · see citing works
“In contrast, mitochondrial fission refers to the process by which a mitochondrion is divided into two separate mitochondria [56].”
BackgroundHypoxia and aging: molecular mechanisms, diseases, and therapeutic targets
Nisar, A., Khan, S., Li, W., Hu, L., Samarawickrama, P. N., Gold, N. M., Zi, M., Mehmood, S. A., Miao, J., & He, Y. (2024) · MedComm · doi:10.1002/mco2.786 · Cited by 32 · see citing works
“19,20 Additionally, hypoxia induces chronic inflammation and cellular senescence, two processes that accelerate the biological aging of tissues.”
Background
- 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 · 2016: 1
- 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
- Health Sciences › Medicine › Epidemiology › 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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