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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.
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“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
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“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
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“However, the over-expression of OPA1 did not improve mitochondrial respiration.(64) Interestingly, knock-down of the mitochondrial fission protein, Drp1, has similar effects on mitochondrial metabolism,(66) suggesting that any alteration in the mitochondrial network appears to impact on metabolism in a negative way.”
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Mitochondrial morphology is altered in atrophied skeletal muscle of aged mice
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“OPA1 is localized to the inner membrane and is primarily involved in inner membrane fusion (Cipolat et al. 2004; Chen et al. 2005).”
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“This latter function has been ascribed to the ongoing dynamics of fusion and fission, which serve to maintain mitochondrial quality control (Chen et al., 2005; Waterham et al., 2007; Zhang and Chan, 2007).”
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The Functional Impact of Mitochondrial Structure Across Subcellular Scales
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The SUMO protease SENP5 is required to maintain mitochondrial morphology and function
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InfluentialMitochondrial Membrane Potential Is Required for MAVS-Mediated Antiviral Signaling
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“DYm has a fundamental role in RLR-induced antiviral responses Having identified that Mfns-dm MEFs were defective in antiviral signaling, we hypothesized that some mitochondrial defect existed in these cells that ultimately led to a dysfunction in cellular signaling, and that DYm could be a candidate, because widesprea…”
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Baker, M. J., Tatsuta, T., & Langer, T. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a007559 · Cited by 271
“The role of fusion in mitochondrial quality control has been highlighted by studies demonstrating that loss of the fusion mediators result in a decline in respiratory chain activity (Chen et al. 2005, 2007).”
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Karbowski, M., & Youle, R. J. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.05.007 · Cited by 256
Oxidative stress and mitochondrial impairment: Key drivers in neurodegenerative disorders
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PKM2 coordinates glycolysis with mitochondrial fusion and oxidative phosphorylation
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BackgroundResultInfluentialAbnormal Mitochondrial Dynamics in the Pathogenesis of Alzheimer's Disease
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“cells defective for fusion display reduced cell growth, decreased mitochondrial membrane potential and defective respiration (Chen et al., 2005).”
Ultrastructure of the Mitochondrion and Its Bearing on Function and Bioenergetics
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Mitochondrial dynamics and disease, OPA1
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BackgroundResultMitochondrial dynamics in the adult cardiomyocytes: which roles for a highly specialized cell?
Piquereau, J., Caffin, F., Novotová, M., Lemaire, C., Veksler, V., Garnier, A., Ventura‐Clapier, R., & Joubert, F. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00102 · Cited by 251
“Disruption of mitochondrial dynamics by overexpression or suppression of fusion (Mfn2, Opa1) (Olichon et al., 2003; Chen et al., 2005) or mitochondrial fission (Benard et al., 2007), can cause alterations in mitochondrial metabolism (Chen and Chan, 2005), according to the degree of differentiation…”
BackgroundDelving deeper: MCL-1's contributions to normal and cancer biology
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“A deficiency in mitochondrial fusion leads to decreased mass and elevated mutation rates of mtDNA and impaired respiratory activity (18, 19).”
BackgroundAmyloid‐Beta Interaction with Mitochondria
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“Unbalanced fusion leads to mitochondrial elongation, and unbalanced fission leads to excessive mitochondrial fragmentation, both of which impair the mitochondrial function [46, 47].”
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Ferri, E., Marzetti, E., Calvani, R., Picca, A., Cesari, M., & Arosio, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155236 · Cited by 224
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“MEF cells were described previously [11,22], and grown at 37uC in Dulbecco’s modified Eagle’s medium (DMEM, Gibco), supplemented with 10% fetal calf serum (FCS, Gibco) and nonessential aminoacids (Sigma).”
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
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Hinton, A. O., Jr., Claypool, S. M., Neikirk, K., Senoo, N., Wanjalla, C. N., Kirabo, A., & Williams, C. R. (2024) · Circulation Research · doi:10.1161/circresaha.124.323800 · Cited by 239
“95 In HF, there is decreased expression of the mitochondrial dynamics regulator MFN2 (eg, in diabetic mice), leading to excessive mitochondrial fission that is linked to the development of HF in rats and humans with pulmonary arterial hypertension.”
BackgroundMitochondrial fragmentation in cigarette smoke-induced bronchial epithelial cell senescence
Hara, H., Araya, J., Ito, S., Kobayashi, K., Takasaka, N., Yoshii, Y., Wakui, H., Kojima, J., Shimizu, K., Numata, T., et al. (2013) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00146.2013 · Cited by 219
OPA1 Mutation and Late‐Onset Cardiomyopathy: Mitochondrial Dysfunction and mtDNA Instability
Chen, L., Liu, T., Tran, A. M. H., Lu, X., Tomilov, A. A., Davies, V. J., Cortopassi, G. A., Chiamvimonvat, N., Bers, D. M., Votruba, M., et al. (2012) · Journal of the American Heart Association · doi:10.1161/jaha.112.003012 · Cited by 237
“Reduction in either MFN1 or MFN2 can be partially compensated for by the other MFN protein, suggesting some overlap in function.(23) Knockout of either MFN1 or MFN2 was protective against ischemia/reperfusion injury in cardiomyocytes,(22,24) whereas a combination knockout of MFN1/2 led to rapidly lethal cardiac failur…”
Mitochondrial dynamics as regulators of cancer biology
Trotta, A. P., & Chipuk, J. E. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2451-3 · Cited by 226
“However, while the mechanism underlying Mfn1 −/− lethality required further investigation, Mfn2 −/− mice died mid-gestation due to reduced trophoblast giant cells in the placenta and resulted in improper placental development, indicating that Mfn1 and Mfn2 are not functionally redundant [6, 7].”
Causal roles of mitochondrial dynamics in longevity and healthy aging
Sharma, A., Smith, H. J., Yao, P., & Mair, W. B. (2019) · EMBO Reports · doi:10.15252/embr.201948395 · Cited by 222
“Additionally, fusion reduces endoplasmic reticulum (ER)-mitochondrial Ca 2+ transfer to prevent Ca 2+ induced cell death [4,45 – 47].”
Critical dependence of neurons on mitochondrial dynamics
Chen, H., & Chan, D. C. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.06.004 · Cited by 219
“Au th or 's pe rs on al co py reduced mitochondrial membrane potential, reduced cellular respiration and even cell death [15 ,24].”
BackgroundInfluentialSelf-citationLoss of Miro1-directed mitochondrial movement results in a novel murine model for neuron disease
Nguyen, T., Oh, S. S., Weaver, D., Lewandowska, A., Maxfield, D., Schuler, M.-H., Smith, N. K., Macfarlane, J. L., Saunders, G. W., Palmer, C. A., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402449111 · Cited by 223
“Lipofectamine 2000 (Invitrogen) was used to transfect either 5 μg of plasmids harboring Myc-tagged variants of Miro1 and Miro2 or 1 μg of a plasmid harboring GFP-OMP25 (provided by the laboratory of D. Chan, California Institute of Technology, Pasadena, CA) (62).”
Mitochondrial Dynamics in Diabetes
Yoon, Y., Galloway, C. A., Jhun, B. S., & Yu, T. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3286 · Cited by 223
“These observations seem contradictory to the general notion that mitochondrial fusion is a requisite for maintaining normal mitochondrial function (29, 31, 32, 147, 179, 184); hence, it would be predicted that DN-Mfn1 inhibits mitochondrial fusion and resulting fragmentation would be associated with mitochondrial dysf…”
Pluripotent stem cell energy metabolism: an update
TeSlaa, T. A., & Teitell, M. A. (2014) · The EMBO Journal · doi:10.15252/embj.201490446 · Cited by 221
“Mitochondrial network fusion status is a determinant of maximal respiratory capacity (Chen et al, 2005; Yu et al, 2006).”
BackgroundMartin, O. J., Lai, L., Soundarapandian, M. M., Leone, T. C., Antonio Zorzano, A., Keller, M. P., Attie, A., Muoio, D. M., & Kelly, D. P. (2013) · Circulation Research · doi:10.1161/circresaha.114.302562 · Cited by 218
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Ryan, Z. C., Craig, T. A., Folmes, C. D. L., Wang, X., Lanza, I. R., Schaible, N., Salisbury, J. L., Nair, K. S., Terzic, A., Sieck, G. C., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.684399 · Cited by 219
Role of mitochondrial dynamics proteins in the pathophysiology of obesity and type 2 diabetes
Zorzano, A., Liesa, M., & Palacín, M. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.02.004 · Cited by 209
Kotiadis, V. N., Duchen, M. R., & Osellame, L. D. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.041 · Cited by 216
“[101–104].”
Mitochondrial dysfunction in amyotrophic lateral sclerosis
Shi, P., Gál, J., Kwinter, D. M., Liu, X., & Zhu, H. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.012 · Cited by 213
“In addition, Mfn1 and Mfn2 deletion results in severe cellular defects, including widespread heterogeneity of mitochondrial membrane potential and decreased cellular respiration [105].”
BackgroundHuman Myo19 Is a Novel Myosin that Associates with Mitochondria
Quintero, O. A., DiVito, M. M., Adikes, R. C., Kortan, M. B., Case, L. B., Lier, A., Panaretos, N. S., Slater, S. Q., Rengarajan, M., Feliu, M., et al. (2009) · Current Biology · doi:10.1016/j.cub.2009.10.026 · Cited by 204
“Defects in their localization and dynamics lead to human disease [3-5].”
Mitochondrial Dynamics in Stem Cells and Differentiation
Seo, B. J., Yoon, S. H., & Tae, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123893 · Cited by 208
“Mouse embryonic fibroblasts (MEFs) defective in mitochondrial fusion could survive, but some of their mitochondria displayed a reduced itochondrial DNA (mtDNA) copy number, a loss of membrane potential, and problems with adenosine triphosphate (ATP) synthesis [14].”
BackgroundLncRNAs regulate metabolism in cancer
Lin, W., Zhou, Q., Wang, C., Zhu, L., Bi, C., Zhang, S., Wang, X., & Jin, H. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.40769 · Cited by 208
“Mitochondrial dynamics has been found to be involved in cell metabolism [27-30].”
BackgroundThe pathophysiology of mitochondrial disease as modeled in the mousePreprint
Wallace, D. C., & Fan, W. (2009) · Genes & Development · doi:10.1101/gad.1784909 · Cited by 204
“During apoptosis, Opa1 is cleaved permitting the cristae to open and facilitating cytochrome c release (Chen et al. 2003, 2005; Cipolat et al. 2004).”
BackgroundPapanicolaou, K. N., Ngoh, G. A., Dabkowski, E. R., O’Connell, K. A., Júnior, R. F. R., Stanley, W. C., & Walsh, K. X. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00833.2011 · Cited by 208
“Disrupting mitochondrial fusion via Mfn-1 or Mfn-2 ablation alters the distribution and morphology of mitochondria and precipitates a stochastic process of mitochondrial dysfunction (9, 10).”
BackgroundThe Role of Mitochondria in the Mechanisms of Cardiac Ischemia-Reperfusion Injury
Kuznetsov, A. V., Javadov, S. A., Margreiter, R., Grimm, M. F., Hagenbuchner, J., & Ausserlechner, M. J. (2019) · Antioxidants · doi:10.3390/antiox8100454 · Cited by 209
Mitochondrial fusion proteins: Dual regulators of morphology and metabolism
Antonio Zorzano, A., Liesa, M., Sebastián, D., Segalés, J., & Palacín, M. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.01.002 · Cited by 204
Mitochondrial dynamics and viral infections: A close nexus
Khan, M. A., Syed, G. H., Kim, S., & Siddiqui, A. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.040 · Cited by 195
“Depletion of bothMfn1 and 2 in cells results in poor cell growth, decreased cellular respiration associated with the heterogeneity of mitochondrial membrane potential [29].”
BackgroundMitofusin2 Mutations Disrupt Axonal Mitochondrial Positioning and Promote Axon Degeneration
Misko, A. L., Sasaki, Y., Tuck, E. J., Milbrandt, J., & Baloh, R. H. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.6338-11.2012 · Cited by 200
“Decreased mitochondrial fusion leads to suppression of mitochondrial function, including loss of membrane potential ( ) and oxidative respiration (Chen et al., 2005).”
Abdullah, C. S., Alam, S., Aishwarya, R., Miriyala, S., Bhuiyan, M. A. N., Panchatcharam, M., Pattillo, C. B., Orr, A. W., Sadoshima, J., Hill, J. A., et al. (2019) · Scientific Reports · doi:10.1038/s41598-018-37862-3 · Cited by 197
Ishihara, T., Ban-Ishihara, R., Maeda, M., Matsunaga, Y., Ichimura, A., Kyogoku, S., Aoki, H., Katada, S., Nakada, K., Nomura, M., et al. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01054-14 · Cited by 200
“Analysis of these mitochondrial fusion factors also revealed a role of intermitochondrial communication in the maintenance of uniformly active mitochondria (4, 5).”
BackgroundPiquereau, J., Caffin, F., Novotová, M., Prola, A., Garnier, A., Matéo, P., Fortin, D., Huynh, L. H., Nicolas, V., Alavi, M. V., et al. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs117 · Cited by 204
“However, almost complete loss of OPA1 resulted in severely altered mitochondrial respiration.(36) The only change in metabolic phenotype found in the present study was an alteration of free fatty acid utilization by mitochondria.”
Diet impact on mitochondrial bioenergetics and dynamics
Putti, R., Sica, R., Migliaccio, V., & Lionetti, L. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00109 · Cited by 192
“Alterations in OPA1 expression also affect mitochondrial bioenergetics, for example Opa1 depletion causes a reduction in basal respiration (Chen et al., 2005).”
BackgroundEmerging Role for Members of the Bcl-2 Family in Mitochondrial Morphogenesis
Autret, A., & Martin, S. J. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.011 · Cited by 196
“For example, fragmentation of mitochondrial networks, through genetic inactivation of Mfn1 and Mfn2 or RNAi-mediated ablation of Opa1, led to markedly decreased rates of respiration (Chen et al., 2005).”
Metalloprotease‐mediated OPA1 processing is modulated by the mitochondrial membrane potential
Guillery, O., Malka, F., Landes, T., Guillou, E., Blackstone, C. D., Lombès, A., Belenguer, P., Arnoult, D., & Rojo, M. (2008) · Biology of the Cell · doi:10.1042/bc20070110 · Cited by 189
“Down-regulation or knock-out of mammalian OPA1 provokes disorganization of inner membrane cristae, induces overall mitochondrial fragmentation and inhibits mitochondrial fusion (Olichon et al., 2003; Griparic et al., 2004; Chen et al., 2005; Song et al., 2007).”
BackgroundRegulation of neuron mitochondrial biogenesis and relevance to brain health
Onyango, I. G., Lu, J., Rodova, M., Lezi, E., Crafter, A. B., & Swerdlow, R. H. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.07.014 · Cited by 190
“mitochondrial fusion and fission [2] that is vital for mitochondrial metabolism, energy production, Ca2+ signaling, reactive oxygen species (ROS) production, apoptosis, and senescence [3-5].”
BackgroundNeutrophil extracellular trap formation requires OPA1-dependent glycolytic ATP production
Amini, P., Stojkov, D., Felser, A., Jackson, C. B., Courage, C., Schaller, A., Gelman, L., Soriano, M. E., Nuoffer, J., Scorrano, L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05387-y · Cited by 190
Dysregulated Mitochondrial Dynamics and Metabolism in Obesity, Diabetes, and Cancer
Dai, W., & Jiang, L. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00570 · Cited by 186
“Mice lacking Mfn1 or Mfn2 are embryonically lethal, which suggests their essential role in embryonic development (7, 18).”
BackgroundBaixauli, F., Martin-Cofreces, N. B., Morlino, G., Carrasco, Y. R., Calabia-Linares, C., Veiga, E., Serrador, J. M., & Sánchez‐Madrid, F. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.25 · Cited by 191
The Mitochondrial Dynamism-Mitophagy-Cell Death Interactome
Dorn, G. W., & Kitsis, R. N. (2014) · Circulation Research · doi:10.1161/circresaha.116.303554 · Cited by 193
“ity, but mitochondria lacking both mitofusin 1 and mitofusin 2 are severely dysmorphic and partially depolarized.(21) David Chan’s group worked around embryonic lethality of germ-”
BackgroundMitochondrial fusion and division: Regulation and role in cell viability
Bénard, G., & Karbowski, M. (2009) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2008.12.012 · Cited by 186
Mitofusin 2 Protects Cerebellar Granule Neurons against Injury-induced Cell Death
Jahani‐Asl, A., Cheung, E. C., Neuspiel, M., MacLaurin, J. G., Fortin, A., Park, D. S., McBride, H. M., & Slack, R. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703812200 · Cited by 187
The ever-growing complexity of the mitochondrial fission machinery
Pagliuso, A., Cossart, P., & Stavru, F. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2603-0 · Cited by 192
“This permits content exchange and enables cross-complementation of mitochondrial DNA molecules, preventing the accumulation of mutant DNA in a specific mitochondrion [5, 6].”
BackgroundLee, H., Smith, S. B., & Yoon, Y. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.762567 · Cited by 190
“Regarding the role of OPA1 in OXPHOS, knockdown or knock-out of OPA1 disrupts cristae structure and respiration and increases apoptotic sensitivity (15, 16, 33, 34), whereas OPA1 overexpression enhances cristae tightness, apoptotic resistance, respiratory supercomplex formation, and OXPHOS (35–38).”
BackgroundMitochondrial Dynamics in Basal and Stressful Conditions
Zemirli, N., Morel, É., & Molino, D. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020564 · Cited by 196
“Also, Mfn1−/− and Mfn2−/− derived MEFs display fragmented MT and are impaired for the production of IFNs and other proinflammatory cytokines in response to viral infection [65].”
Background
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
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