The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction
Open accessAbstract
Mitochondria undergo continual cycles of fusion and fission, and the balance of these opposing processes regulates mitochondrial morphology. Paradoxically, cells invest many resources to maintain tubular mitochondrial morphology, when reducing both fusion and fission simultaneously achieves the same end. This observation suggests a requirement for mitochondrial fusion, beyond maintenance of organelle morphology. Here, we show that cells with targeted null mutations in Mfn1 or Mfn2 retained low levels of mitochondrial fusion and escaped major cellular dysfunction. Analysis of these mutant cells showed that both homotypic and heterotypic interactions of Mfns are capable of fusion. In contrast, cells lacking both Mfn1 and Mfn2 completely lacked mitochondrial fusion and showed severe cellular defects, including poor cell growth, widespread heterogeneity of mitochondrial membrane potential, and decreased cellular respiration. Disruption of OPA1 by RNAi also blocked all mitochondrial fusion and resulted in similar cellular defects. These defects in Mfn-null or OPA1-RNAi mammalian cells were corrected upon restoration of mitochondrial fusion, unlike the irreversible defects found in fzodelta yeast. In contrast, fragmentation of mitochondria, without severe loss of fusion, did not result in such cellular defects. Our results showed that key cellular functions decline as mitochondrial fusion is progressively abrogated.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“fibroblasts lacking Mfn1 and Mfn2 completely lack mitochondrial fusion and show severe cellular defects, including poor growth, heterogeneity of mitochondrial membrane potential, and decreased respiration (11).”
From Mitochondrial Fission Contributes to Mitochondrial Dysfunction and Insulin Resistance in Skeletal Muscle (2012) · cites this paper as [11]
In the citing paper
“This is of particular importance since it is now established that mitochondrial morphology and function are interrelated, with changes in mitochondrial morphology affecting mitochondrial function (Chen et al., 2005; Jahani-Asl et al., 2007; Yu et al., 2008; Ong et al., 2010; Gomes et al., 2011) and vice versa (Benard et al., 2007).”
From Effects of Aging and Caloric Restriction on Fiber Type Composition, Mitochondrial Morphology and Dynamics in Rat Oxidative and Glycolytic Muscles (2019) · cites this paper as Chen et al., 2005
In the citing paper
“Repression of Mfn2 in cells decreases oxygen consumption, glucose oxidation, mitochondrial membrane potential and the expression of oxidative phosphorylation proteins (Bach et al., 2003; Chen et al., 2005; Pich et al., 2005).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Chen et al., 2005
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
A System for Stable Expression of Short Interfering RNAs in Mammalian Cells
Brummelkamp, T. R., Bernards, R., & Agami, R. (2002) · Science · doi:10.1126/science.1068999 · Cited by 4,295
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-citationMutations 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
Delettre, C., Lenaers, G., Griffoin, J.-M., Gigarel, N., Lorenzo, C., Belenguer, P., Pelloquin, L., Grosgeorge, J., Turc-Carel, C., Perret, E., et al. (2000) · Nature Genetics · doi:10.1038/79936 · Cited by 1,446
Alexander, C., Votruba, M., Pesch, U. E. A., Thiselton, D. L., Mayer, S., Moore, A., Rodriguez, M., Kellner, U., Leo-Kottler, B., Auburger, G., et al. (2000) · Nature Genetics · doi:10.1038/79944 · Cited by 1,330
OPA1 requires mitofusin 1 to promote mitochondrial fusion
Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407043101 · Cited by 1,300
Olichon, A., Baricault, L., Gas, N., Guillou, E., Valette, A., Belenguer, P., & Lenaers, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200677200 · Cited by 1,168
Control of mitochondrial morphology by a human mitofusin
Santel, A., & Fuller, M. T. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.5.867 · Cited by 1,012
Structural Basis of Mitochondrial Tethering by Mitofusin Complexes
Koshiba, T., Detmer, S. A., Kaiser, J. T., Chen, H., McCaffery, J. M., & Chan, D. C. (2004) · Science · doi:10.1126/science.1099793 · Cited by 910
Self-citationThe dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast
Bleazard, W., McCaffery, J. M., King, E. J., Bale, S., Mozdy, A. D., Tieu, Q., Nunnari, J. M., & Shaw, J. M. (1999) · Nature Cell Biology · doi:10.1038/13014 · Cited by 795
Flagged first, then by citations
Research works printed but not linked: 1
- Bakeeva, 1981, Eur. J. Cell Biol., 25, 175
Cited by
Sorted by citations
Items 901–1,000 of 1,000
Vecchis, D. D., Brandner, A. F., Baaden, M., Cohen, M. M., & Taly, A. (2019) · The Journal of Membrane Biology · doi:10.1007/s00232-019-00089-y · Cited by 20
Perciavalle, R. M. (2012) · doi:10.21007/etd.cghs.2012.0242 · Cited by 17
The Role of Mitochondrial Dynamin in Stroke
Li, C., Chen, C., Qin, H., Ao, C., Chen, J., Tan, J., & Zeng, L. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2504798 · Cited by 19
“MFN2 is a GTPase on the mitochondrial outer membrane, which is essential for maintaining intracellular homeostasis [63, 86].”
BackgroundTan, L. X., Li, J., Germer, C. J., & Lakkaraju, A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1044672 · Cited by 17
Cytoskeletal and Cytoskeleton-Associated Proteins: Key Regulators of Cancer Stem Cell Properties
Li, Y., Wang, D., Ge, H., Güngör, C., Gong, X., & Chen, Y. (2022) · Pharmaceuticals · doi:10.3390/ph15111369 · Cited by 17
Preservation of the quality and fertility potential of post-thawed rooster sperm using MitoQ
Alipour‐Jenaghard, P., Daghigh-Kia, H., & Masoudi, R. (2023) · Theriogenology · doi:10.1016/j.theriogenology.2023.06.014 · Cited by 19
Choppa, V. S. R., & Kim, W. K. (2023) · Biomolecules · doi:10.3390/biom13071032 · Cited by 17
Fully automated software for quantitative measurements of mitochondrial morphology
McClatchey, P. M., Keller, A. C., Bouchard, R. J., Knaub, L. A., & Reusch, J. E. B. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.12.003 · Cited by 17
“…body of research is unsurprising in light of recent reports indicating that mitochondrial dynamics are involved in regulating cellular respiration (Chen et al., 2005), calcium dynamics (Rizzuto et al., 2012), free radical production (Yu et al., 2006), substrate catabolism (Liesa and Shirihai,…”
BackgroundMAMs are attractive targets for bacterial repurposing of the host cell
Escoll, P., Rolando, M., & Buchrieser, C. (2016) · BioEssays · doi:10.1002/bies.201600171 · Cited by 17
“Mitochondrial morphology has important implications on the bioenergetic status of the organelle, as disruption of mitochondrial fusion impairs electron transport chain function [28].”
BackgroundKatz, M. G., Gubara, S. M., Hadas, Y., Weber, T., Kumar, A., Eliyahu, E., Bridges, C. R., & Fargnoli, A. S. (2019) · Journal of Thoracic and Cardiovascular Surgery · doi:10.1016/j.jtcvs.2019.08.089 · Cited by 17
Ferver, A., Greene, E., Wideman, R. F., Jr., & Dridi, S. (2021) · Frontiers in Veterinary Science · doi:10.3389/fvets.2021.640901 · Cited by 17
“Mitochondrial fusion is a state in which separate mitochondrial organelles fuse into a larger network and is often seen during stress conditions as it has the capacity to partially mix damaged mitochondria for complementation (28, 29).”
BackgroundJin, H., Qi, F., Chu, F., Liu, C., Qian, T., Zeng, W., Wang, Q., Wang, X., & Xiao, J. (2021) · Phytotherapy Research · doi:10.1002/ptr.7234 · Cited by 17
“Microtubule stabilization and axon regeneration must be supported by energy, and mitochondria are the main organelles that produce energy, affecting microtubule stability and growth cone migration (Chen et al., 2005; Misko et al., 2010; Rodríguez-Martín et al., 2016).”
BackgroundHuang, W., Jou, M., & Tsung, I. P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081546 · Cited by 17
“Elongated mitochondria have enhanced mitochondrial respiration capacity and hyperpolarized ΔΨm, which may be better equipped to withstand the metabolic stresses associated with H/RO injury [62,63].”
BackgroundWalczak, J., Partyka, M., Duszyński, J., & Szczepanowska, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-14964-y · Cited by 19
Popkov, V. A., Plotnikov, E. Y., Lyamzaev, K. G., Silachev, D. N., Zorova, L. D., Pevzner, I. B., Jankauskas, S. S., Zorov, S. D., Babenko, V. А., & Zorov, D. B. (2015) · Biochemistry (Moscow) · doi:10.1134/s000629791505003x · Cited by 17
“Over recent years, it has become clear that mito chondrial heterogeneity is particularly accounted for by two coupled processes – mitochondrial dynamics (mito chondrial fragmentation and fusion) [27] and autophagy (mitophagy) [12, 28].”
Regulation of PGC-1α and PGC-1α-responsive genes with forskolin-induced Schwann cell differentiation
Cowell, R. M., Blake, K. R., Inoue, T., & Russell, J. W. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.04.104 · Cited by 17
“Mitochondrial homeostasis requires a delicate balance between fission and fusion, the disturbance of which can lead to decreased cellular respiration, decreased cell growth, and cell death [2,7,8,28].”
BackgroundXu, M., Feng, P., Yan, J., & Li, L. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1474310 · Cited by 19
Chen, X., & Xu, Y. (2009) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-009-0603-5 · Cited by 16
“The Mfn2 protein is localized in the outer mitochondrial membrane, and participates in mitochondrial fusion events and aids in the regulation of mitochondrial metabolism [8, 9 ] . Recent studies show that physiologic and pathophysiologic conditions that are characterized by altered glucose oxidation (diabetes, obesity…”
BackgroundHeras, N. D. L., & Lahera, V. (2021) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-021-02638-8 · Cited by 19
“However, a low activity in oxidative phosphorylation is correlated with fragmented mitochondria with very small intracrest spaces [49, 51].”
BackgroundMitochondrial DNA Depletion Syndrome and Its Associated Cardiac Disease
Wang, H., Han, Y., Li, S., Chen, Y., Chen, Y., Wang, J., Zhang, Y., Zhang, Y., Wang, J., Xia, Y., et al. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.808115 · Cited by 18
“Mitochondrial dynamics is often determined by the dynamic balances between fission and fusion as well as between biogenesis and degradation such as mitochondrial phagocytosis (27).”
BackgroundApproaches to Mitigate Mitochondrial Dysfunction in Sensorineural Hearing Loss
Okur, M. N., & Djalilian, H. R. (2022) · Annals of Biomedical Engineering · doi:10.1007/s10439-022-03103-y · Cited by 18
Fish Models for Exploring Mitochondrial Dysfunction Affecting Neurodegenerative Disorders
Otsuka, T., & Matsui, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087079 · Cited by 17
Mitochondrial Drugs for Alzheimer Disease
Bonda, D., Wang, X., Gustaw‐Rothenberg, K., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Pharmaceuticals · doi:10.3390/ph2030287 · Cited by 16
“Within a healthy neuron, a delicate balance of fission and fusion is necessary for cellular integrity [69–74].”
Imaging of Mitochondrial Dynamics in Motor and Sensory Axons of Living Mice
Bolea, I., Gan, W., Manfredi, G., & Magrané, J. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801415-8.00006-0 · Cited by 15
Mitochondrial dynamics and metabolism in induced pluripotency
Prieto, J., Ponsoda, X., Belmonte, J. C. I., & Torres, J. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.110870 · Cited by 18
Effects of Mitochondrial Dynamics in the Pathophysiology of Obesity
Wang, J., Lin, X., Zhao, N., Dong, G., Wu, W., Huang, K., & Fu, J. (2022) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2703107 · Cited by 16
Effects of Long-Term Exposure to Copper on Mitochondria-Mediated Apoptosis in Pig Liver
Hu, Z., Liao, J., Zhang, K., Huang, K., Li, Q., Lei, C., Han, Q., Zhang, H., Guo, J., Hu, L., et al. (2022) · Biological Trace Element Research · doi:10.1007/s12011-022-03303-6 · Cited by 16
“Studies have shown that the underperformance of mitochondrial function is associated with the impediment of mitochondrial fusion [53].”
BackgroundRyu, S., Choi, K., Park, J., Park, Y., Kim, S., & Choi, C. (2012) · Cancer Letters · doi:10.1016/j.canlet.2012.03.038 · Cited by 16
“Knockout of Mfn1 or Mfn2 resulted in mitochondrial fragmentation [11]; however, Mfn1 and Mfn2 displayed distinct types of mitochondrial fragmentation and had different GTPase activities [11,43,46].”
Mitochondrial dysfunction is induced by the overexpression of UCP4 in 3T3-L1 adipocytes
Guo (2009) · International Journal of Molecular Medicine · doi:10.3892/ijmm_00000315 · Cited by 16
Frtús, A., Smolková, B., Uzhytchak, M., Lunová, M., Jirsa, M., Petrenko, Y., Dejneka, A., & Lunov, O. (2023) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.2c01518 · Cited by 15
Paraquat-induced neurogenesis abnormalities via Drp1-mediated mitochondrial fission
Zhang, B., Zhang, Y., Zuo, Z., Xiong, G., Luo, H., Song, B., Zhao, L., Zhou, Z., & Chang, X. (2023) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2023.114939 · Cited by 15
Mitochondrial Dynamics in Pulmonary Hypertension
Santos, E. W., Khatoon, S., Mise, A. D., Zheng, Y., & Wang, Y.-X. (2023) · Biomedicines · doi:10.3390/biomedicines12010053 · Cited by 15
“Under these conditions, mitochondria may not receive sufficient substrates, such as acetyl-CoA and O 2 , inducing major changes in structure, function, and dynamics [60].”
BackgroundGreiner, T. U., Koh, A., Peris, E., Bergentall, M., Johansson, M., Hansson, G. C., Drucker, D. J., & Bäckhed, F. (2024) · Molecular Metabolism · doi:10.1016/j.molmet.2024.101924 · Cited by 19
“An excessive fragmentation of mitochondria can be associated with impaired mitochondrial function [37,38] and reduced respiration leading to increased oxygen levels.”
BackgroundBacteria–organelle communication in physiology and disease
Lee, Y.-T., Şentürk, M., Guan, Y., & Wang, M. C. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202310134 · Cited by 15
Mitochondrial fusion in Chlamydomonas reinhardtii zygotes
Scholz, D., & Westermann, B. (2012) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2012.10.004 · Cited by 15
Operation of mitochondrial machinery in viral infection-induced immune responses
Lai, J., Luo, S., & Ho, L. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.08.044 · Cited by 16
“The introduction of OPA1 RNA interference results in an interruption of mitochondrial fusion and similar cellular defects [37].”
InfluentialSon, Y., Jeong, Y. I., Hwang, K. C., Jeong, Y. I., & Hwang, W. S. (2021) · Theriogenology · doi:10.1016/j.theriogenology.2021.01.010 · Cited by 15
MFN1 and MFN2 Are Dispensable for Sperm Development and Functions in Mice
Miao, J., Chen, W., Wang, P., Zhang, X., Wang, L., Wang, S., & Wang, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413507 · Cited by 15
Specific Changes in Morphology and Dynamics of Plant Mitochondria under Abiotic Stress
Tang, H., & Zhu, H. (2022) · Horticulturae · doi:10.3390/horticulturae9010011 · Cited by 15
Mitochondrial retention of Opa1 is required for mouse embryogenesis
Moore‐Scott, B. A., Aviles, G. D. G., Larkins, C. E., Hillman, M. J., & Caspary, T. (2010) · Mammalian Genome · doi:10.1007/s00335-010-9272-8 · Cited by 15
“Mitochondrial fragmentation in the MEFs was similar to mitochondrial fragmentation in cell lines from patients with heterozygous mutations in Opa1 as well as cell lines in which Opa1 expression was knocked down by siRNA (Amati-Bonneau et al. 2005, 2008, 2009; Chen et al. 2005; Cipolat et al. 2004; Griparic et al. 2004…”
BackgroundMethodInfluentialProteolytic regulation of mitochondrial dynamics
Dietz, J. V., Bohovych, I., Viana, M. P., & Khalimonchuk, O. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.04.008 · Cited by 15
Zhao, H., Yin, R. H., Wang, Y., Lee, Y., Luo, T., Zhang, J., Qiu, H., Ambrose, S. L., Wang, L., Ren, J., et al. (2017) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2017.09.017 · Cited by 15
Falfushynska, H., & Sokolova, I. M. (2023) · Biology Open · doi:10.1242/bio.060069 · Cited by 14
“As an example, early mitochondrial swelling and loss of the mitochondrial membrane potential associated with lower activity of respiratory complexes led to poor cell growth, decreased cellular respiration, and caspase-3-mediated cell death in hypoxic neurons (Niquet et al., 2003; Chen et al., 2005).”
Wang, G., Lu, W., Shen, W., Karbowski, M., Kaushal, S., & Yang, P. (2024) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2023.11.008 · Cited by 14
Combustion-derived particles inhibit in vitro human lung fibroblast-mediated matrix remodeling
Bové, H., Devoght, J., Rasking, L., Peters, M., Slenders, E., Roeffaers, M. B. J., Jorge-Peñas, Á., Oosterwyck, H. V., & Ameloot, M. M. (2018) · Journal of Nanobiotechnology · doi:10.1186/s12951-018-0410-x · Cited by 14
Dey, S., Eisa, A. A., Kline, D., Wagner, F. F., Abeysirigunawardena, S. C., & Vijayaraghavan, S. (2019) · The FASEB Journal · doi:10.1096/fj.201902163r · Cited by 16
Rapid manipulation of mitochondrial morphology in a living cell with iCMM
Miyamoto, T., Uosaki, H., Mizunoe, Y., Han, S., Goto, S., Yamanaka, D., Masuda, M., Yoneyama, Y., Nakamura, H., Hattori, N., et al. (2021) · Cell Reports Methods · doi:10.1016/j.crmeth.2021.100052 · Cited by 14
“Tomaintain bioenergetic activity in this process, mitochondria go through repeated fusion and fission cycles (Chen et al., 2005; Rapaport et al., 1998; Twig et al., 2008).”
BackgroundObara, K., Yoshikawa, T., Yamaguchi, R., Kuwata, K., Nakatsukasa, K., Nishimura, K., & Kamura, T. (2022) · Nature Communications · doi:10.1038/s41467-022-29704-8 · Cited by 14
Delettre, C., Hamel, C., & Lenaers, G. (2015) · Europe PMC (PubMed Central) · Cited by 14
Modelling biochemical features of mitochondrial neuropathology
Bird, M., Thorburn, D. R., & Frazier, A. E. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.017 · Cited by 14
“Stunted dendritic arbor growth & impaired ability to different into Purkinje cells [87,131,132]”
BackgroundEl papel de la mitocondria en el dolor de la neuropatía diabética
Hernández-Beltrán, N., Moreno, C. B., & Gutiérrez‐Álvarez, Á. M. (2012) · Endocrinología y Nutrición · doi:10.1016/j.endonu.2012.03.005 · Cited by 14
Mitochondrial metabolism in aging: Effect of dietary interventions
Cerqueira, F. M., & Kowaltowski, A. J. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2012.03.009 · Cited by 14
Charcot-Marie-Tooth Disease: Seventeen Causative Genes
Lee, J. H., & Choi, B. (2006) · Journal of Clinical Neurology · doi:10.3988/jcn.2006.2.2.92 · Cited by 14
“Mitofusin 2 encodes an outer mitochondrial membrane protein which, in cooperation with the MFN1 isoform, has important roles in the regulation of mitochondrial fusion,(53-55) a function essential for metabolic activity in eukaryotic cells.(56) It has also been suggested that MFN2 may be associated with maintaining mit…”
BackgroundMitochondrial Dynamics: Shaping Metabolic Adaptation
Cantó, C. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.05.004 · Cited by 15
Investigating the role of Sirtuins in cell reprogramming
Shin, J., Kim, J., Park, H., & Kim, J. (2018) · BMB Reports · doi:10.5483/bmbrep.2018.51.10.172 · Cited by 14
Lee, D. G., Kim, K., Lee, H., Bae, Y. C., Huh, J., Lee, S., & Lee, D. (2019) · NeuroToxicology · doi:10.1016/j.neuro.2019.08.003 · Cited by 14
Hefnawy, A., Negreira, G. H., Jara, M., Cotton, J. A., Maes, I., D’haenens, E., Imamura, H., Cuypers, B., Monsieurs, P., Mouchtoglou, C., et al. (2022) · mBio · doi:10.1128/mbio.03264-21 · Cited by 14
Emerging role of the cardiac lipidome in the progression of heart failure
Flori, L., Calderone, V., & Testai, L. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118385 · Cited by 14
Mitohormesis and mitochondrial dynamics in the regulation of stem cell fate
Barzegari, A., Aboulhassanzadeh, S., Landon, R., Gueguen, V., Meddahi‐Pellé, A., Parvizpour, S., Anagnostou, F., & Pavon‐Djavid, G. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30820 · Cited by 14
“Fusion‐mediated mitochondrial‐ component‐sharing lends support to the multiple elements of mitochondrial biology, mtDNA integrity (Ono et al., 2001), mitochondrial respiration (Chen et al., 2005), Δψm equilibration (Twig et al., 2008), apoptosis and signaling events like Ca2+ oscillations.”
BackgroundLei, K., Wu, R., Wang, J., Lei, X., Zhou, E., Fan, R., & Gong, L. (2023) · Translational Stroke Research · doi:10.1007/s12975-023-01191-z · Cited by 14
“Under normal circum-stances, mitochondrial fusion maintains organelle integrity through the diffusion and sharing of components [32].”
BackgroundYegambaram, M., Sun, X., Flores, A. G., Lü, Q., Soto, J. E., Richards, J., Aggarwal, S., Wang, T., Gu, H., Fineman, J. R., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417533 · Cited by 14
“Mitochondrial dysfunction can result from the dysregulation of mitochondrial fission/fusion dynamics [18,19].”
BackgroundZhuang, Y., Jiang, W., Zhao, Z., Li, W., Deng, Z., & Liu, J. (2024) · Channels · doi:10.1080/19336950.2024.2335467 · Cited by 14
“For example, Mfn1−/− and Mfn2−/− cells exhibit widespread mitochondrial fragmentation but still survive completely [72], indicating that mitochondrial division based on the expression of mitochondrial dynamics genes is not always related to cell apoptosis.”
BackgroundRole of mitofusin 2 in cardiovascular oxidative injury
Zheng, M., & Xiao, R. (2010) · Journal of Molecular Medicine · doi:10.1007/s00109-010-0675-5 · Cited by 14
“Over the past decade, increasing evidence has shown that, in addition to regulating mitochondrial morphology, mitochondrial fusion/fission participates in various vital biological processes, such as mitochondrial biogenesis [1], maintenance of mitochondrial DNA [2], cell metabolism [3], cell proliferation [4], and cel…”
Tang, Q., Ding, C., Xu, Q., Bai, Y., Qiao, X., Wang, K., & Fang, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.585166 · Cited by 14
“These opposing processes work in concert to maintain the shape, size, and number of mitochondria and their physiological function (Chan, 2012), and mitochondrial dynamics contribute to mitochondrial respiration (Chen et al., 2005; Zorzano et al., 2010).”
BackgroundMonitoring Mitochondrial Function in Aedes albopictus C6/36 Cell Line during Dengue Virus Infection
Santana-Román, M. E., Maycotte, P., Uribe‐Carvajal, S., Uribe‐Alvarez, C., Alvarado-Medina, N., Khan, M. A., Siddiqui, A., & Pando‐Robles, V. (2021) · Insects · doi:10.3390/insects12100934 · Cited by 15
“Cells lacking MFN1, MFN2 and OPA1 completely lacked mitochondrial fusion and showed severe cellular defects, including poor cell growth, loss of MMP, decreased cellular respiration, and apoptosis [53].”
BackgroundZhao, M., Lian, A., Zhong, L., & Guo, R. (2022) · Acta Physiologica · doi:10.1111/apha.13757 · Cited by 14
Pandey, A. K., Sarkar, S., Yadav, S. K., Yadav, S., Srikrishna, S., Siddiqui, M. H., Parmar, D., & Yadav, S. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02667-5 · Cited by 13
“These findings are in line with previous research which discovered that depletion of MFNs or OPA-1 reduces OCR and mitochondrial proton leak in mouse fibroblasts and myoblasts [66, 67].”
ResultRobb, E. L., Christoff, C. A., Maddalena, L. A., & Stuart, J. A. (2013) · Canadian Journal of Zoology · doi:10.1139/cjz-2013-0131 · Cited by 13
“In contrast, mitochondria isolated from mouse cells lacking the fusion enzymes mitofusin (Mfn) 1 and Mfn2 have a lower membrane potential and a reduced capacity for oxidative phosphorylation (Chen et al. 2005).”
BackgroundCan short-term fasting protect against doxorubicin-induced cardiotoxicity?
Dirks‐Naylor, A. J. (2014) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v5.i3.269 · Cited by 13
Cerium oxide nanozyme modulate the ‘exercise’ redox biology of skeletal muscle
Arya, A., Sethy, N. K., Gangwar, A., Bhargava, N., Dubey, A., Roy, M., Srivastava, G. K., Singh, S. K., Das, M., & Bhargava, K. (2017) · Materials Research Express · doi:10.1088/2053-1591/aa6922 · Cited by 13
Pavlik, L. L., Mikheeva, I. B., Al’-Mugkhrabi, Y. M., Berest, V. P., Kirova, Y. I., Germanova, E. L., Lukyanova, L. D., & Mironova, G. D. (2018) · Bulletin of Experimental Biology and Medicine · doi:10.1007/s10517-018-3993-1 · Cited by 15
Role of GTPases in the regulation of mitochondrial dynamics in Parkinson's disease
Zhang, X., Huang, W., Fan, Y.-Y., Sun, Y. J., & Ge, X. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.06.005 · Cited by 14
Axonal transport dysfunction of mitochondria in traumatic brain injury: A novel therapeutic target
Shin, S. S., Karlsson, M., Mazandi, V. M., Ranganathan, A., Hallowell, T., Delso, N., & Kilbaugh, T. J. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113311 · Cited by 13
Resveratrol protects the mitochondria from vitrification injury in mouse 2-cell embryos
Gao, Z., Yao, G., Zhang, H., Liu, H., Yang, Z., Liu, C., Li, W., Zhao, X., Wei, Q., & Ma, B. (2020) · Cryobiology · doi:10.1016/j.cryobiol.2020.05.007 · Cited by 13
Can ethics be taught? An essay.
Pellegrino, E. D. (1989) · PubMed · Cited by 13
Abdellaoui, A., Gouzi, F., Notarnicola, C., Bourret, A., Suc, A., Laoudj‐Chenivesse, D., Héraud, N., Mercier, J. G., PREFAUT, C. G., Hayot, M., et al. (2025) · Acta Physiologica · doi:10.1111/apha.70079 · Cited by 13
“…by the fusion/fission ratio, improved in both groups following ET (Figure 3G), suggesting that ET can enhance mitochondrial quality control mechanisms even in COPD, potentially aiding in the removal of damaged mitochondria and the maintenance of mitochondrial function, such as respiration [33, 34].”
BAX regulates dendritic spine development via mitochondrial fusion
Gu, Q., Duan, K., Petralia, R. S., Wang, Y., & Li, Z. (2022) · Neuroscience Research · doi:10.1016/j.neures.2022.06.002 · Cited by 13
Esmaeilkhanian, S., Asadzadeh, N., & Masoudi, R. (2023) · Cryobiology · doi:10.1016/j.cryobiol.2022.11.238 · Cited by 12
Mitochondria in Multi-Directional Differentiation of Dental-Derived Mesenchymal Stem Cells
Liu, H., Xu, K., He, Y., & Huang, F. P. (2023) · Biomolecules · doi:10.3390/biom14010012 · Cited by 13
“Importantly, any insufficiency or malfunction of these proteins can significantly impair mitochondrial fusion, thus leading to consequential defects in mitochondrial function [26].”
BackgroundDiéguez, H. H., Romeo, H. E., Alaimo, A., Aguirre, N. A. B., Calanni, J. S., Areán, J. S. A., Álvarez, S., Sciurano, R. B., Rosenstein, R. E., & Dorfman, D. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.03.024 · Cited by 13
del Campo, C. M. Z.-M., Rosas, M., & Guarner‐Lans, V. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051456 · Cited by 12
Sun, X., Zeng, C., Wang, F., Zhang, Z., Yang, F., Liu, Z., Li, K., & Zhang, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113402 · Cited by 12
“A previous study found that the down-regulation of OPA1 or the invalidation of MFN1 and MFN2 strongly decreased mitochondrial respiratory capacity in cells when fueled with substrate for electron transport chain complexes I, II, and IV [35,36].”
BackgroundXi Tao, X. U., Yang, B., Zhang, H., Feng, X., Hao, H., Du, W., Zhu, H., Khan, A. A., Khan, M. Z., Zhang, P., et al. (2023) · Antioxidants · doi:10.3390/antiox12050991 · Cited by 12
“Finally, the mRNA expression levels of genes associated with lipid synthesis (SREBP1, FABP3, and PPARG) of bovine oocytes, ROS level, mRNA expression levels of genes Antioxidants 2023, 12, 991 5 of 18 involved in ER stress (GRP78, XBP1, and ATF4) and mitochondrial function (MFN1, MFN2, DRP1, and FIS1), and apoptosis l…”
BackgroundInfluentialCardiac mitochondrial dynamics: miR-mediated regulation during cardiac injury
Sivakumar, A., Subbiah, R., Balakrishnan, R., & Rajendhran, J. (2017) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2017.07.003 · Cited by 13
Margvelani, G., Meparishvili, M., Tevdoradze, E., McCabe, B., & Solomonia, R. (2017) · NeuroReport · doi:10.1097/wnr.0000000000000936 · Cited by 9
Flight duration and flight muscle ultrastructure of unfed hawk moths
Wone, B. W. M., Pathak, J., & Davidowitz, G. (2018) · Arthropod Structure & Development · doi:10.1016/j.asd.2018.05.003 · Cited by 12
“Fusion of aging mitochondria is thought to affect mtDNA integrity and respiratory function ( )Chen et al., 2005 and is controlled by the optic atrophy 1 ( ) gene and the twoOpa1 GTPases mitofusin 1 and 2 (isoforms Mfn1 and Mfn2) in humans ( …”
Function and regulation of mitofusin 2 in cardiovascular physiology and pathology
Yu, F., Xu, T., Wang, M., Chang, W., Li, P., & Wang, J. (2018) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2018.07.003 · Cited by 12
Lin, T., Chang, Y., Lin, H., Liou, C., Wang, P., Chuang, J., Chen, S., Chuang, Y., Huang, S., Hsu, T., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0224173 · Cited by 12
Apoptosis inducing factor: Cellular protective function in Dictyostelium discoideum
Kadam, A. A., Mehta, D., Jubin, T., Mansuri, M. S., & Begum, R. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148158 · Cited by 12
Esmaeilkhanian, S., Asadzadeh, N., & Masoudi, R. (2021) · Cryobiology · doi:10.1016/j.cryobiol.2021.09.008 · Cited by 12
Mitochondria: a new focus as an anti‐aging target in skin care
Menon, G. K., Farra, C. D., Botto, J.-M., & Domloge, N. (2010) · Journal of Cosmetic Dermatology · doi:10.1111/j.1473-2165.2010.00496.x · Cited by 13
Quantifying Heterogeneity of Individual Organelles in Mixed Populations via Mass Cytometry
Brown, H. M., & Arriaga, E. A. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b02790 · Cited by 13
Tsoneva, E., & Yordanov, A. D. (2025) · Cells · doi:10.3390/cells14201629 · Cited by 11
“Approaches that normalize mitochondrial dynamics-for instance, Drp1 inhibitors to limit excessive fission or compounds that promote fusion-might restore healthier networks and resensitize HPV+ cells to apoptosis “[21–23]”.”
Hassanzadeh, S., Sabetvand, M., Sardar, R., Aryanpour, R., & Namjoo, Z. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03710-3 · Cited by 11
“…the mitochondrial networks are highly orchestrated in some cells, it is not unexpected that the morphology of mitochondria can significantly affect their function due to their functional characteristics in the respiratory chain and regulation of nuclear and mitochondrial gene expression [10, 11].”
UCP2 and pancreatic cancer: conscious uncoupling for therapeutic effect
Caggiano, E. G., & Taniguchi, C. M. (2024) · Cancer and Metastasis Reviews · doi:10.1007/s10555-023-10157-4 · Cited by 13
“However, the survival advantage that this grants PDAC cells is not entirely understood, especially considering that the loss of fusion or fission alone results in severe cellular defects [160, 183], and fission is normally a marker of cell stress [157].”
BackgroundXiao, Y., Zhang, Y., Xie, K., Huang, X., Liu, X., Luo, J., & Tan, S. (2024) · International Journal of Biological Sciences · doi:10.7150/ijbs.90835 · Cited by 13
“Mitochondria are highly dynamic organelles characterized by a high frequency of fission and fusion events [16], whereas disruption of mitochondrial fission and fusion leads to mitochondrial heterogeneity and dysfunction [17, 18].”
BackgroundMfn2-dependent fusion pathway of PE-enriched micron-sized vesicles
Peñalva, D. A., Monnappa, A. K., Natale, P., & López‐Montero, I. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313609121 · Cited by 11
“Though this might suggest a certain redundancy (21), it was shown that Mfn1 and Mfn2 exhibit differences in their expression patterns throughout different tissues (10, 15, 17, 22), nucleotide - binding affinity and hydrolysis rate (11, 19), and posttranslational modifications (23, 24).”
BackgroundMitochondrial Dysfunctions: Genetic and Cellular Implications Revealed by Various Model Organisms
Stańczyk, M., Szubart, N., Maślanka, R., & Zadrąg‐Tęcza, R. (2024) · Genes · doi:10.3390/genes15091153 · Cited by 12
“[53].”
BackgroundRegulation 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
Mitochondrial Function and Neurodegenerative Diseases
Wilkins, H. M., Weidling, I., Koppel, S., Wang, X., von Schulze, A., & Swerdlow, R. H. (2018) · The Molecular and Cellular Basis of Neurodegenerative Diseases · doi:10.1016/b978-0-12-811304-2.00013-4 · Cited by 2
Metadata
- Authors
- Chen, H., Chomyn, A., & Chan, D. C.
- Affiliations
- California Institute of Technology (US)
- Corresponding author
- Chan, David C.
- ORCID
- Chan, David C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-07
- Volume
- 280
- Issue
- 28
- Pages
- 26185-26192
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2124140045
- Cited by
- 1,376
- References
- 28
- Citations by year
- 2026: 32 · 2025: 53 · 2024: 55 · 2023: 61 · 2022: 63 · 2021: 77 · 2020: 84 · 2019: 79 · 2018: 95 · 2017: 89 · 2016: 56 · 2015: 74 · 2014: 78 · 2013: 70 · 2012: 92
- FWCI
- 15.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- Muscular Dystrophy Association
- United Mitochondrial Disease Foundation
- National Institutes of Health
- National Institute of General Medical Sciences (GM11726, 1 R01 GM62967-01, R01GM062967)
- 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, Mfn1, mitofusin 2, OPA1, mitochondrial heterogeneity, mitochondrial membrane potential, cellular respiration, mitochondrial morphology, mitochondrial dysfunction
- MeSH terms
- Alleles, Animals, Fibroblasts, Genotype, Membrane Potentials, Microscopy, Fluorescence, Mitochondria, Mutation, Oxygen, Oxygen Consumption, Polyethylene Glycols, Recombinant Fusion Proteins, RNA, Time Factors, Blotting, Western, Microscopy, Confocal, GTP Phosphohydrolases, RNA Interference, Cell Proliferation, Green Fluorescent Proteins, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
