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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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Cites
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601
Self-citationMitochondria and cell death: outer membrane permeabilization and beyond
Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593
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
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
The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755
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
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Neikirk, K., Stephens, D. C., Beasley, H. K., Marshall, A. G., Gaddy, J. A., Damo, S. M., & Hinton, A. O., Jr. (2024) · BioTechniques · doi:10.2144/btn-2023-0072 · Cited by 12
Dalmao‐Fernández, A., Hermida‐Gómez, T., Nogueira-Recalde, U., Rego‐Pérez, I., Blanco, F. J., & Fernández-Moreno, M. (2024) · Cells · doi:10.3390/cells13110976 · Cited by 13
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Wang, X., Liu, Y., Wang, J., Lu, X., Guo, Z., Lv, S., Sun, Z., Gao, T., Gao, F., & Yuan, J. (2024) · Reproductive Sciences · doi:10.1007/s43032-024-01634-4 · Cited by 12
“This leads to the formation of a ring structure at the fission site, subsequent GTP hydrolysis, and contraction of the DRP1 helix to sever the mitochondria, completing division [5, 36, 39, 40].”
del Campo, C. M. Z.-M., Rosas, M., & Guarner‐Lans, V. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051456 · Cited by 12
“Epigenetic programming by environmental factors regulates the biogenesis of mitochondria, which undergo repeated cycles of fission and fusion [58].”
BackgroundInfluentialCrocker, C. L., Baumgarner, B. L., & Kinsey, S. T. (2019) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-019-09568-0 · Cited by 13
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BackgroundLi, W., Pan, W., Huang, M., Yang, Z., He, Y., Zhang, W., Zhang, J., Gu, Z., Zhang, D., Yan, W., et al. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c04658 · Cited by 12
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“In mitochondrial fusion, homo- and hetero-oligomeric structures are formed by Mfn1 and Mfn2 to link two neighboring mitochondria for outer membrane fusion, and OPA1 directly promotes inner membrane fusion (Chan, 2012).”
BackgroundMutlu, N., Garipler, G., Akdoğan, E., & Dunn, C. D. (2014) · G3 Genes Genomes Genetics · doi:10.1534/g3.114.010330 · Cited by 11
“at both the outer membrane (OM) and the inner membrane (IM) of mitochondria (Hoppins and Nunnari 2009; Chan 2012).”
BackgroundPlant mitochondrial dynamics and the role of membrane lipids
Pan, R., & Hu, J. (2015) · Plant Signaling & Behavior · doi:10.1080/15592324.2015.1050573 · Cited by 12
“Animal and yeast mitochondria often appear highly tubular and interconnected, which reflects the dominance of mitochondrial fusion in these organisms.(40) The mitochondrial fusion machineries are well characterized in these systems with the core components being members of the DRP family as well.”
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Zanfardino, P., Doccini, S., Santorelli, F. M., & Petruzzella, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158325 · Cited by 13
Foster, C. R., Satomi, S., Kato, Y., & Patel, H. H. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190388 · Cited by 12
Tsoneva, E., & Yordanov, A. D. (2025) · Cells · doi:10.3390/cells14201629 · Cited by 11
“This balance is regulated by key proteins, with Drp1 (dynamin-related protein 1) driving fission, and OPA1 together with MFN1 and MFN2 mediating fusion [5,6].”
Holloway, C., Zhong, G. G., Kim, Y., Ye, H., Sampath, H., Hämmerling, U., Isoherranen, N., & Quadro, L. (2022) · The FASEB Journal · doi:10.1096/fj.202101910rr · Cited by 10
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“Additionally, mitochondria can go through fusion and fission events, which involves the physical merging of several mitochondria to form one large mitochondrion, and the separation of a mitochondrion into several mitochondria, respectively (Chan 2012).”
BackgroundPharmacological Progress of Mitophagy Regulation
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Napolitano, G., Fasciolo, G., Tomajoli, M. T. M., & Venditti, P. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512453 · Cited by 12
Pang, X., Li, T., Shi, R.-J., Wan, Z., Tang, Y., Tang, Y., & Liang, X. (2023) · Molecular Carcinogenesis · doi:10.1002/mc.23635 · Cited by 11
“42,43 Studies have demonstrated the interaction of mitochondria fission/fusion with cancer progression and metastasis.”
BackgroundATAD1 inhibits hepatitis C virus infection by removing the viral TA‐protein NS5B from mitochondria
Zhou, Q. S., Yang, Y., Xu, Z., Deng, K., Zhang, Z., Hao, J., Li, N., Wang, Y., Wang, Z., Chen, H., et al. (2023) · EMBO Reports · doi:10.15252/embr.202256614 · Cited by 11
“Mitochondria are highly dynamic organelles that constantly undergo fission (fragmentation), fusion, and mitophagy to maintain mitochondrial quality control (Chan, 2012).”
Islam, M. N., Mishra, V. K., Munalisa, R., Parveen, F., Ali, S. F., Akter, K., Ahmed, T., Ho, T., & Huang, C. (2024) · Molecular & Cellular Toxicology · doi:10.1007/s13273-023-00424-4 · Cited by 11
“Increased apoptosis in CVD due to the fragmentation of mitochondrial network Mitochondria are dynamic organelles that undergo continual fission and fusion to adapt to changes in the cellular environment (Chan 2012; Suarez-Rivero et al. 2016; Tilokani et al. 2018).”
Regulation of Mitoflash Biogenesis and Signaling by Mitochondrial Dynamics
Li, W., Sun, T., Liu, B., Wu, D., Qi, W., Wang, X., Ma, Q., & Cheng, H. (2016) · Scientific Reports · doi:10.1038/srep32933 · Cited by 11
Vo, M., Ko, M. S., Lee, U. H., Yoon, E. H., Lee, B. J., Cho, W. J., Ha, C. M., Kim, K., & Park, J. W. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.03.154 · Cited by 11
“As a main regulator of mitochondrial fission, Drp1 activity is regulated by several post-translational modifications, such as phosphorylation, S-nitrosylation, SUMOylation, and ubiquitination [26,27].”
BackgroundShen, F., Weng, S., Tsai, M., Su, Y., Li, S., Chang, S., Chen, J., Chang, Y., Liou, C., Lin, T., et al. (2021) · Journal of Diabetes Investigation · doi:10.1111/jdi.13629 · Cited by 11
Zhao, M., Han, M., Liang, L., Song, Q., Li, X., Du, Y., Hu, D., Cheng, Y., Wang, Q. K., & Ke, T. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166429 · Cited by 11
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BackgroundInfluentialSihali-Beloui, O., Aroune, D., Benazouz, F., Hadji, A., El-Aoufi, S., & Marco, S. (2019) · Comptes Rendus Biologies · doi:10.1016/j.crvi.2019.04.003 · Cited by 11
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Qiu, T.-X., Wang, H., Liu, L., & Chen, J. (2022) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2022.114331 · Cited by 10
Zhang, Z., Bie, X., Chen, Z., Liu, J., Xie, Z., Li, X., Xiao, M., Zhang, Q., Zhang, Y., Yang, Y., et al. (2024) · BMC Pediatrics · doi:10.1186/s12887-023-04442-y · Cited by 11
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BackgroundLu, J., Liu, G., Sun, W., Jia, G., Zhao, H. Y., Chen, X., & Wang, J. (2024) · Journal of Nutrition · doi:10.1016/j.tjnut.2024.03.001 · Cited by 10
Ye, F., Wei, C., & Wu, A. (2024) · Annals of Medicine · doi:10.1080/07853890.2024.2411012 · Cited by 11
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“The fusion protein optic atrophy protein 1 (OPA1) is located on the inner mitochondrial membrane (IMM) while GTPase mitofusin1 and 2 (Mfn1/2) are located on the outer mitochondrial membrane (OMM) [97,100–104].”
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Zhu, Q., McElroy, R., Machhar, J. S., Cassel, J. A., Zheng, Z., Mansoori, B., Guo, H., Guo, S., Pangilinan, C. R., Liang, J., et al. (2025) · Nature Microbiology · doi:10.1038/s41564-025-02018-3 · Cited by 9
Ma, J., Yuan, M., Guo, S., Gao, T., Li, C., & Liu, L. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.08.027 · Cited by 9
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Richhariya, S., Shin, D., Schlichting, M., & Rosbash, M. (2025) · Current Biology · doi:10.1016/j.cub.2025.09.063 · Cited by 13
Yu, X., Li, M., & Li, H. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118846 · Cited by 13
Chang, Y., Wu, Y., Jiang, X., Zhu, J., Wang, C., Ma, R., & Li, G. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/9251835 · Cited by 9
“The central player in mitochondrial fi ssion is DRP1 [13].”
Talk to Me—Interplay between Mitochondria and Microbiota in Aging
Endres, K., & Friedland, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310818 · Cited by 9
“However, aging of mitochondria cannot be seen as clear as for bacteria, or even for eukaryotic cells, due to their specific biology: mitochondria not only undergo fission, but they also fuse, and this continuous and fast exchange of organelle content (“kiss and run”) can lead to preservation of a coherent population (…”
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“The delicate dynamic balance between fission and fusion is critical for maintaining optimal mitochondrial function and meeting specific metabolic and energetic cellular demands following ischemic brain injury [125].”
BackgroundRegulation of mitochondrial inner membrane fusion: divergent evolution with similar solutions?
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BackgroundKrishnan, R., Jeena, K., & Prasad, K. P. (2018) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2018.07.003 · Cited by 9
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Caldwell, K. A., Thies, J. L., & Caldwell, G. A. (2018) · Metabolites · doi:10.3390/metabo8040070 · Cited by 9
“Since abnormal mitochondrial fission/fusion is associated with ∆Ψm collapse [75,76], we decided to explore whether the metabolite altered the regular fission/fusion cycles that are regulated by the GTPases (Drp1 and Opa1) and mitofusins (Mfn1/Mfn2) that are located on the outer and inner mitochondrial membranes.”
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Murdocca, M., Spitalieri, P., Cappello, A., Colasuonno, F., Moreno, S., Candi, E., D’Apice, M. R., Novelli, G., & Sangiuolo, F. C. (2022) · Aging · doi:10.18632/aging.203910 · Cited by 9
“Mitochondria are part of a comprehensive network maintained by a sophisticate balance between mitochondrial biogenesis, fission and fusion, and mitophagy [24, 25].”
BackgroundDridi, H., Yehya, M., Barsotti, R., Liu, Y., Reiken, S. R., Azria, L., Yuan, Q., Bahlouli, L., Soni, R. K., Marks, A. R., et al. (2023) · PNAS Nexus · doi:10.1093/pnasnexus/pgad336 · Cited by 9
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BackgroundSword, J., Fomitcheva, I. V., & Kirov, S. A. (2024) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x241257887 · Cited by 9
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Kritskaya, K. A., Fedotova, E. I., & Berezhnov, A. V. (2024) · Biomedicines · doi:10.3390/biomedicines12020282 · Cited by 8
“To eliminate the toxic effects of dysfunctional mitochondria, organisms have developed a complex system of mitochondrial quality control implemented through the processes of mitochondrial fission/fusion [2] and the regulation of mitochondrial biogenesis and mitophagy.”
BackgroundDelerue, T., Khosrobakhsh, F., Daloyau, M., Emorine, L. J., Dedieu, A., Herbert, C. J., Bonnefoy, N., Pelloquin, L., & Belenguer, P. (2016) · FEBS Letters · doi:10.1002/1873-3468.12432 · Cited by 8
Mitochondrial Fission and Fusion
Hewitt, V. L., & Whitworth, A. J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803783-6.00003-1 · Cited by 10
Yong, M., Chen, H., & Chan, D. C. (2018) · PLoS Currents · doi:10.1371/currents.hd.a4e15b80c4915c828d39754942c6631f · Cited by 10
Ko, J., Rounds, S., & Lü, Q. (2020) · Pulmonary Circulation · doi:10.1177/2045894020924994 · Cited by 9
“Key proteins involved in mitochondrial fission, such as dynamin-related protein 1 (Drp1), and mitochondrial fusion, such as Mitofusin 1 and 2 (Mfn1 and Mfn2), are essential for cell survival.(39,41) Mice deficient in either Mfn1 and Mfn2 die in midgestation, and interruption of mitochondrial fusion results in loss of…”
BackgroundChen, X., Liang, J., Bin, W., Luo, H., & Yang, X. (2021) · Cardiovascular Toxicology · doi:10.1007/s12012-021-09691-w · Cited by 8
Plasticity of perisynaptic astroglia during ischemia-induced spreading depolarization
Fomitcheva, I. V., Sword, J., Shi, Y., & Kirov, S. A. (2022) · Cerebral Cortex · doi:10.1093/cercor/bhac434 · Cited by 8
Song, M., Zhang, J., Huo, S., Zhang, X., Cui, Y., & Li, Y. (2023) · Food and Chemical Toxicology · doi:10.1016/j.fct.2023.113762 · Cited by 9
Zhang, S., Li, Y., Zhu, W., Zhang, L., Lei, L., Tian, X., Chen, K. G., Shi, W., & Cong, B. (2023) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17901 · Cited by 8
“14,15 Mitochondria are highly dynamic organelles that interact with other organelles, such as the endoplasmic reticulum, to communicate informa - tion.”
BackgroundMironova, G. D., Rozova, E. V., Belosludtseva, N. V., & Man’kovskaya, I. N. (2019) · Bulletin of Experimental Biology and Medicine · doi:10.1007/s10517-019-04445-9 · Cited by 8
Natural and Artificial Mechanisms of Mitochondrial Genome Elimination
Zakirova, E. G., Muzyka, V. V., Mazunin, I., & Orishchenko, К. E. (2021) · Life · doi:10.3390/life11020076 · Cited by 9
“Recruited enzymes ubiquitinate mitofusins (MFNs) and other proteins located at the OMM and are responsible for its fusion [58].”
BackgroundBa, Q., & Yang, G. (2017) · Frontiers in Biology · doi:10.1007/s11515-016-1436-9 · Cited by 8
“An important line of evidence comes from studies of mitochondrial fusion and fission (Chan, 2012; Youle and van der Bliek, 2012) as well as transport and anchoring mediated spatial distribution (Frederick and Shaw, 2007; Sheng and Cai, 2012; Sheng, 2014).”
InfluentialGupte, T. M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126829 · Cited by 8
“Mitochondrial morphology is maintained by a balance of fission and fusion [1], allowing mitochondrial fragmentation to be achieved either by inhibiting fusion or by increasing fission.”
BackgroundChen, P., Chang, C., Lin, W., Nagabhushanam, K., Ho, C., & Pan, M. (2022) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202101077 · Cited by 8
Metabolic consequences of PGC-1α dysregulation in adult zebrafish muscle
Kurchaba, N. W., Charette, J. M., & LeMoine, C. M. R. (2022) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00188.2021 · Cited by 8
Neuronal glycolysis meets mitophagy to govern organismal wellbeing
Jiménez-Blasco, D., Lapresa, R., Agulla, J., Almeida, Á., & Bolaños, J. P. (2025) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2025.05.005 · Cited by 8
Peixoto-Rodrigues, M. C., Borges-Martins, V. P. P., Monteiro-Neto, J. R., Vicente, B., Guimarães, L. J., Carvalho, C. F., Galina, A., Midlej, V. D. V. P., Toborek, M. J., Hauser‐Davis, R. A., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103862 · Cited by 7
“Interference with the equilibrium between these processes can lead to fragmented or hyperfused mitochondria, resulting in cellular dysfunction [6].”
Zhang, Y., Han, H., Zhang, T., Zhang, T., Ma, L., Yang, Z. R., & Zhao, Y. (2025) · Biomolecules · doi:10.3390/biom15091292 · Cited by 8
Mitochondrial dysfunction as the “mother” of all hallmarks of aging
Weissig, V. (2025) · Journal of Mitochondria Plastids and Endosymbiosis · doi:10.1080/28347056.2025.2560191 · Cited by 9
Chaudhari, M., Makhloufi, J., Doelling, B., Kataria, R., Bhatnagar, A., Kalra, D. K., & Baba, S. P. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27062886 · Cited by 9
“Other proteins involved in the fission process include dynamin 2, human mitochondrial dynamics proteins 49 and 51, mitochondrial fission factor 1 protein (MFP1), and mitochondrial fission factor (MFF) [47–50].”
Yu, C., Peng, Z.-Q., Wang, T., Qu, X.-H., Yang, P. C., Huang, S.-R., Jiang, L.-P., Tou, F., & Han, X. (2023) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2023247 · Cited by 7
“Instead, mitochondrial fission produces a large number of small and broken mitochondria, which are implicated in the stress response and apoptosis [11].”
BackgroundCastellaneta, A., Losito, I., Porcelli, V., Barile, S., Maresca, A., Dotto, V. D., Losacco, V., Guadalupi, L. S., Calvano, C. D., Chan, D. C., et al. (2024) · Journal of Lipid Research · doi:10.1016/j.jlr.2024.100563 · Cited by 7
“Fission allows for the isolation of excessively deteriorated mitochondria to be targeted for autophagic removal by fusing with lysosomes (12, 13).”
BackgroundWang, Y., Lin, S., Chen, L., Li, M., Zhu, Z., Zhuang, Z., Cai, M., Zhang, H., Xing, C., Li, W., et al. (2024) · Nano Research · doi:10.1007/s12274-024-6758-3 · Cited by 9
Vidyadharan, V. A., Betancourt, A., Smith, C., Blesson, C. S., & Yallampalli, C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252312860 · Cited by 10
Almeida, L. O., Goto, R. N., Neto, M. P. C., Sousa, L. O., Curti, C., & Leopoldino, A. M. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.01.104 · Cited by 7
Varmazyad, M., Modi, M. M., Kalen, A. L., Sarsour, E. H., Wagner, B. A., Du, J., Schultz, M. K., Buettner, G. R., Pigge, F. C., & Goswami, P. C. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.050 · Cited by 9
Liu, Z., Chiang, C. ‐., Nip, J., Feng, L., Zhang, Y., Rocha, S., & Georgakoudi, I. (2021) · Biomedical Optics Express · doi:10.1364/boe.432561 · Cited by 7
From dynamin related proteins structures and oligomers to membrane fusion mediated by mitofusins
Ozeir, M., & Cohen, M. M. (2022) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2022.148913 · Cited by 7
Willin/FRMD6 Mediates Mitochondrial Dysfunction Relevant to Neuronal Aβ Toxicity
Chen, D., Yu, W., Aitken, L., & Gunn‐Moore, F. J. (2022) · Cells · doi:10.3390/cells11193140 · Cited by 7
“Because mitochondrial fission and fusion play critical roles in the maintenance of mitochondrial function [45,46], we next evaluated mitochondrial morphology using an unbiased deep-learning based segmentation and analysis tool, MitoSegNet [38].”
BackgroundMethodKang, Y. S., Seong, D., Kim, J.-C., & Kim, S. H. (2020) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph17155461 · Cited by 8
Mitochondrial Maintenance in Skeletal MusclePreprint
de Smalen, L. M., & Handschin, C. (2024) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041514 · Cited by 12
Chen, Y.-A., Lu, W.-N., Li, P., Nie, T., Li, Y., Zeng, R., Lin, S., Gao, M., Hejtmancik, J. F., Hou, L., et al. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.07.025 · Cited by 6
Abdel‐Razik, R. K., Mosallam, E. M., & Hamed, N. (2022) · Alexandria Science Exchange Journal · doi:10.21608/asejaiqjsae.2022.223119 · Cited by 6
“…activate a chain of events such as reduced transcription and partial assembly of the electron transport chain (ETC) complexes, which leads to decreased ETC activity, thus lowering ATP synthesis, increased reactive oxygen species (ROS) production, and apoptosis (Gredilla et al., 2010; Chan, 2012).”
Background
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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