Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion

Song, Zhiyin; Ghochani, Mariam; McCaffery, J. Michael; Frey, Terrence G.; Chan, David C.

doi:10.1091/mbc.e09-03-0252

Cited by 623Mitochondrial Function and PathologyAutophagy in Disease and TherapyATP Synthase and ATPases Research

Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion

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Song, Zhiyin, Ghochani, Mariam, McCaffery, J. Michael, Frey, Terrence G., Chan, David C.·2009·Molecular Biology of the Cell

DOI 10.1091/mbc.e09-03-0252PMC PMC2719570

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Abstract

Mitochondrial fusion requires the coordinated fusion of the outer and inner membranes. Three large GTPases--OPA1 and the mitofusins Mfn1 and Mfn2--are essential for the fusion of mammalian mitochondria. OPA1 is mutated in dominant optic atrophy, a neurodegenerative disease of the optic nerve. In yeast, the OPA1 ortholog Mgm1 is required for inner membrane fusion in vitro; nevertheless, yeast lacking Mgm1 show neither outer nor inner membrane fusion in vivo, because of the tight coupling between these two processes. We find that outer membrane fusion can be readily visualized in OPA1-null mouse cells in vivo, but these events do not progress to inner membrane fusion. Similar defects are found in cells lacking prohibitins, which are required for proper OPA1 processing. In contrast, double Mfn-null cells show neither outer nor inner membrane fusion. Mitochondria in OPA1-null cells often contain multiple matrix compartments bounded together by a single outer membrane, consistent with uncoupling of outer versus inner membrane fusion. In addition, unlike mitofusins and yeast Mgm1, OPA1 is not required on adjacent mitochondria to mediate membrane fusion. These results indicate that mammalian mitofusins and OPA1 mediate distinct sequential fusion steps that are readily uncoupled, in contrast to the situation in yeast.

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Depletion of any one of Mfn1, Mfn2 or OPA1 results in severe dysfunction in respiratory capacity and fragmentation of mitochondria.
“Depletion of any of one these proteins results in severe dysfunction in respiratory capacity and fragmentation of mitochondria (Chen et al., 2005; Chen et al., 2010; Song et al., 2009)”
From Role of the mitochondrial DNA replication machinery in mitochondrial DNA mutagenesis, aging and age-related diseases (2017) · cites this paper as Song et al., 2009

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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 · see citing works
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Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T., Bartoli, D., Polishuck, R. S., Danial, N. N., De Strooper, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.025 · Cited by 1,673 · see citing works
A Photoactivatable GFP for Selective Photolabeling of Proteins and Cells
Patterson, G. H., & Lippincott‐Schwartz, J. (2002) · Science · doi:10.1126/science.1074952 · Cited by 1,612 · 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
Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy
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 · 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
OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28
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 · see citing works
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 · see citing works
Mitochondrial dynamics and apoptosis
Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270 · see citing works
Loss of OPA1 Perturbates the Mitochondrial Inner Membrane Structure and Integrity, Leading to Cytochrome c Release and Apoptosis
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 · 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
Mitochondrial fusion protects against neurodegeneration in the cerebellum
Chen, H., McCaffery, J. M., & Chan, D. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.026 · Cited by 924 · see citing works
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 · see citing works
OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L
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
The Machines that Divide and Fuse Mitochondria
Hoppins, S., Lackner, L., & Nunnari, J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.071905.090048 · Cited by 790 · 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 Morphology and Dynamics in Yeast and Multicellular Eukaryotes
Okamoto, K., & Shaw, J. M. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.093019 · Cited by 737 · see citing works
Prohibitins control cell proliferation and apoptosis by regulating OPA1-dependent cristae morphogenesis in mitochondriaPreprint
Merkwirth, C., Dargazanli, S., Tatsuta, T., Geimer, S., Löwer, B., Wunderlich, F. T., von Kleist-Retzow, J., Waisman, A., Westermann, B., & Langer, T. (2008) · Genes & Development · doi:10.1101/gad.460708 · Cited by 519 · see citing works
Mitochondrial Inner-Membrane Fusion and Crista Maintenance Requires the Dynamin-Related GTPase Mgm1
Meeusen, S., DeVay, R. M., Block, J., Cassidy-Stone, A., Wayson, S. M., McCaffery, J. M., & Nunnari, J. M. (2006) · Cell · doi:10.1016/j.cell.2006.09.021 · Cited by 474 · see citing works
Loss of the Intermembrane Space Protein Mgm1/OPA1 Induces Swelling and Localized Constrictions along the Lengths of Mitochondria
Griparić, L., van der Wel, N. N., Orozco, I. J., Peters, P. J., & van der Bliek, A. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400920200 · Cited by 468 · see citing works
Opa1 deficiency in a mouse model of autosomal dominant optic atrophy impairs mitochondrial morphology, optic nerve structure and visual function
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
Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis
Karbowski, M., Arnoult, D., Chen, H., Chan, D. C., Smith, C. L., & Youle, R. J. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200309082 · Cited by 433 · see citing works
Mutation of OPA1 causes dominant optic atrophy with external ophthalmoplegia, ataxia, deafness and multiple mitochondrial DNA deletions: a novel disorder of mtDNA maintenance
Hudson, G., Amati-Bonneau, P., Blakely, E. L., Stewart, J. D., He, L., Schaefer, A. M., Griffiths, P. G., Ahlqvist, K., Suomalainen, A., Reynier, P., et al. (2008) · Brain · doi:10.1093/brain/awm272 · Cited by 428 · see citing works
OPA1 mutations associated with dominant optic atrophy impair oxidative phosphorylation and mitochondrial fusion
Zanna, C., Ghelli, A. M., Porcelli, A. M., Karbowski, M., Youle, R. J., Schimpf, S., Wissinger, B., Pinti, M., Cossarizza, A., Vidoni, S., et al. (2007) · Brain · doi:10.1093/brain/awm335 · Cited by 334 · see citing works
Correlated three-dimensional light and electron microscopy reveals transformation of mitochondria during apoptosis
Sun, M., Williams, J. M., Muñoz‐Pinedo, C., Perkins, G. A., Brown, J. M., Ellisman, M. H., Green, D. R., & Frey, T. (2007) · Nature Cell Biology · doi:10.1038/ncb1630 · Cited by 279 · see citing works
A splice site mutation in the murine Opa1 gene features pathology of autosomal dominant optic atrophy
Alavi, M. V., Bette, S. J., Schimpf, S., Schuettauf, F., Schraermeyer, U., Wehrl, H. F., Rüttiger, L., Beck, S. C., Tonagel, F., Pichler, B. J., et al. (2006) · Brain · doi:10.1093/brain/awm005 · Cited by 278 · 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
The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion
Wong, E. D., Wagner, J. A., Scott, S. V., Okreglak, V., Holewinske, T. J., Cassidy-Stone, A., & Nunnari, J. M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200209015 · Cited by 255 · see citing works
Separate fusion of outer and inner mitochondrial membranes
Malka, F., Guillery, O., Cifuentes-Díaz, C., Guillou, E., Belenguer, P., Lombès, A., & Rojo, M. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400488 · Cited by 233 · see citing works
Ugo1p Links the Fzo1p and Mgm1p GTPases for Mitochondrial Fusion
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Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein
Nemoto, Y., & Camilli, P. V. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.11.2991 · Cited by 195 · see citing works
OPA1 (Kjer Type) Dominant Optic Atrophy: A Novel Mitochondrial Disease
Delettre, C., Lenaers, G., Pelloquin, L., Belenguer, P., & Hamel, C. (2002) · Molecular Genetics and Metabolism · doi:10.1006/mgme.2001.3278 · Cited by 191 · see citing works
Mitochondrial outer and inner membrane fusion requires a modified carrier protein
Hoppins, S. C., Horner, J. S., Song, C., McCaffery, J. M., & Nunnari, J. M. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200809099 · Cited by 93 · see citing works
Molecular Genetics of Autosomal-Dominant Axonal Charcot-Marie-Tooth Disease
Zuchner, S. L., & Vance, J. M. (2006) · NeuroMolecular Medicine · doi:10.1385/nmm:8:1-2:63 · Cited by 79 · see citing works
OPA1 mutations and mitochondrial DNA damage: keeping the magic circle in shape
Zeviani, M. (2008) · Brain · doi:10.1093/brain/awm339 · Cited by 41 · see citing works
Conventional and Immunoelectron Microscopy of Mitochondria
Perkins, E. M., & McCaffery, J. M. (2007) · Methods in molecular biology · doi:10.1007/978-1-59745-365-3_33 · Cited by 34 · see citing works
PA‐GFP: A Window into the Subcellular Adventures of the Individual Mitochondrion
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Mitochondria
(2007) · Methods in molecular biology · doi:10.1007/978-1-59745-365-3 · Cited by 6 · see citing works

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Hoppins, S. C., Edlich, F., Harwig, M. C., Banerjee, S., McCaffery, J. M., Youle, R. J., & Nunnari, J. M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.11.030 · Cited by 243 · see citing works
The MFN2 gene is responsible for mitochondrial DNA instability and optic atrophy 'plus' phenotype
Rouzier, C., Bannwarth, S., Chaussenot, A., Chevrollier, A., Verschueren, A., Bonello‐Palot, N., Fragaki, K., Caño, A., Pouget, J., Pellissier, J., et al. (2011) · Brain · doi:10.1093/brain/awr323 · Cited by 243 · see citing works
OPA1 Isoforms in the Hierarchical Organization of Mitochondrial Functions
Dotto, V. D., Mishra, P., Vidoni, S., Fogazza, M., Maresca, A., Caporali, L., McCaffery, J. M., Cappelletti, M., Baruffini, E., Lenaers, G., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.073 · Cited by 243 · see citing works
OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation
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
Physiological functions of mitochondrial fusion
Chen, H., & Chan, D. C. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05615.x · Cited by 221 · see citing works
Alterations in Mitochondrial Quality Control in Alzheimer’s Disease
Cai, Q., & Tammineni, P. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00024 · Cited by 215 · see citing works
Insulin Stimulates Mitochondrial Fusion and Function in Cardiomyocytes via the Akt-mTOR-NFκB-Opa-1 Signaling Pathway
Parra, V., Verdejo, H., Iglewski, M., del Campo, A., Troncoso, R., Jones, D., Zhu, Y., Kuzmicic, J., Pennanen, C., López‐Crisosto, C., et al. (2013) · Diabetes · doi:10.2337/db13-0340 · Cited by 219 · see citing works
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 216 · see citing works
Mutant SOD1G93A triggers mitochondrial fragmentation in spinal cord motor neurons: Neuroprotection by SIRT3 and PGC-1α
Song, W., Song, Y., Kincaid, B., Bossy, B., & Bossy‐Wetzel, E. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.07.004 · Cited by 215 · see citing works
A Role for Peroxisome Proliferator-Activated Receptor γ Coactivator-1 in the Control of Mitochondrial Dynamics During Postnatal Cardiac Growth
Martin, O. J., Lai, L., Soundarapandian, M. M., Leone, T. C., Zorzano, A., Keller, M. P., Attie, A., Muoio, D. M., & Kelly, D. P. (2013) · Circulation Research · doi:10.1161/circresaha.114.302562 · Cited by 213 · see citing works
Mutations in SLC25A46, encoding a UGO1-like protein, cause an optic atrophy spectrum disorder
Abrams, A. J., Hufnagel, R. B., Rebelo, A. P., Zanna, C., Patel, N., Gonzalez, M., Campeanu, I. J., Griffin, L. B., Groenewald, S., Strickland, A. V., et al. (2015) · Nature Genetics · doi:10.1038/ng.3354 · Cited by 204 · see citing works
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 201 · see citing works
Mitochondrial hyperfusion induced by loss of the fission protein Drp1 causes ATM-dependent G2/M arrest and aneuploidy through DNA replication stress
Qian, W., Choi, S., Gibson, G. A., Watkins, S. C., Bakkenist, C. J., & Houten, B. V. (2012) · Journal of Cell Science · doi:10.1242/jcs.109769 · Cited by 198 · see citing works
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 192 · see citing works
Mitochondrial quality control mechanisms as molecular targets in diabetic heart
Chang, X., Li, Y., Cai, C., Wu, F., He, J., Zhang, Y., Zhong, J., Tan, Y., Liu, R., Zhu, H., et al. (2022) · Metabolism · doi:10.1016/j.metabol.2022.155313 · Cited by 192 · see citing works
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 188 · see citing works
The Mitochondrial Dynamism-Mitophagy-Cell Death Interactome
Dorn, G. W., & Kitsis, R. N. (2014) · Circulation Research · doi:10.1161/circresaha.116.303554 · Cited by 185 · see citing works
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 184 · see citing works
The short variant of the mitochondrial dynamin OPA1 maintains mitochondrial energetics and cristae structure
Lee, H., Smith, S. B., & Yoon, Y. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.762567 · Cited by 190 · see citing works
Mitochondrial Dynamics in Basal and Stressful Conditions
Zemirli, N., Morel, É., & Molino, D. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020564 · Cited by 186 · see citing works
Mitochondrial fission and fusion
Lee, H., & Yoon, Y. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160129 · Cited by 183 · see citing works
Mitochondrial dynamics in the regulation of neurogenesis: From development to the adult brain
Khacho, M., & Slack, R. S. (2017) · Developmental Dynamics · doi:10.1002/dvdy.24538 · Cited by 185 · see citing works
Mitochondrial network structure homeostasis and cell death
Xie, L., Shi, F., Tan, Z., Li, Y., Bode, A. M., & Cao, Y. (2018) · Cancer Science · doi:10.1111/cas.13830 · Cited by 178 · see citing works
Role of the mitochondrial DNA replication machinery in mitochondrial DNA mutagenesis, aging and age-related diseases
DeBalsi, K. L., Hoff, K. E., & Copeland, W. C. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.006 · Cited by 180 · see citing works
Mitochondrial Biogenesis in Neurons: How and Where
Cardanho‐Ramos, C., & Morais, V. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222313059 · Cited by 179 · see citing works
Mitochondrial dynamics in Parkinson's disease: a role for α-synuclein?
Devoto, V. M. P., & Falzone, T. L. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.026294 · Cited by 180 · see citing works
Is Mitochondrial Dysfunction a Common Root of Noncommunicable Chronic Diseases?
Díaz‐Vegas, A., Sánchez-Aguilera, P., Krycer, J. R., Morales, P. E., Monsalves‐Álvarez, M., Cifuentes, M., Rothermel, B. A., & Lavandero, S. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnaa005 · Cited by 174 · see citing works
Mic60/Mitofilin determines MICOS assembly essential for mitochondrial dynamics and mtDNA nucleoid organization
Li, H., Ruan, Y., Zhang, K., Jian, F., Hu, C., Miao, L., Gong, L., Sun, L., Zhang, X., Chen, S., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.102 · Cited by 171 · 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
The dynamin-related GTPase Opa1 is required for glucose-stimulated ATP production in pancreatic beta cells
Zhang, Z., Wakabayashi, N., Wakabayashi, J., Tamura, Y., Song, W., Sereda, S., Clerc, P., Polster, B. M., Aja, S. M., Pletnikov, M. V., et al. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-12-0933 · Cited by 170 · see citing works
The role of alterations in mitochondrial dynamics and PGC‐1α over‐expression in fast muscle atrophy following hindlimb unloading
Cannavino, J., Brocca, L., Sandri, M., Grassi, B., Bottinelli, R., & Pellegrino, M. A. (2015) · The Journal of Physiology · doi:10.1113/jphysiol.2014.286740 · Cited by 166 · see citing works
Why size matters – balancing mitochondrial dynamics in Alzheimer's disease
DuBoff, B., Feany, M. Β., & Götz, J. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.03.002 · Cited by 164 · see citing works
Functions of outer mitochondrial membrane proteins: mediating the crosstalk between mitochondrial dynamics and mitophagy
Xian, H., & Liou, Y. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00657-z · Cited by 166 · see citing works
Kissing and nanotunneling mediate intermitochondrial communication in the heart
Huang, X., Sun, L., Ji, S., Zhao, T. S., Zhang, W., Xu, J., Zhang, J., Wang, Y., Wang, X., Franzini‐Armstrong, C., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300741110 · Cited by 164 · see citing works
Unravelling the mechanisms regulating muscle mitochondrial biogenesis
Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159 · see citing works
Mitochondrial dynamics in heart disease
Dorn, G. W. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.03.008 · Cited by 159 · see citing works
Redox homeostasis, oxidative stress and mitophagy
Garza-Lombó, C., Pappa, A., Panayiotidis, M. I., & Franco, R. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.01.002 · Cited by 161 · see citing works
Membrane depolarization activates the mitochondrial protease OMA1 by stimulating self‐cleavage
Zhang, K., Li, H., & Song, Z. (2014) · EMBO Reports · doi:10.1002/embr.201338240 · Cited by 159 · see citing works
Mitochondrial fission is required for cardiomyocyte hypertrophy via a Ca2+-calcineurin signalling pathway
Pennanen, C., Parra, V., López‐Crisosto, C., Morales, P. E., del Campo, A., Gutiérrez, T., Rivera-Mejías, P., Kuzmicic, J., Chiong, M., Zorzano, A., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.139394 · Cited by 157 · see citing works
Mitochondrial Dynamics and Mitochondrial Dysfunction in Diabetes.
Wada, J., & Nakatsuka, A. (2016) · PubMed · doi:10.18926/amo/54413 · Cited by 157 · see citing works
Contribution of Tau Pathology to Mitochondrial Impairment in Neurodegeneration
Maria Jose Perez, J., Jara, C., & Quintanilla, R. A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00441 · Cited by 153 · see citing works
Mitochondrial dynamics and cell death in heart failure
Marı́n-Garcı́a, J., & Akhmedov, A. T. (2016) · Heart Failure Reviews · doi:10.1007/s10741-016-9530-2 · Cited by 154 · see citing works
Functional and morphological impact of ER stress on mitochondria
Vannuvel, K., Renard, P., Raes, M. J., & Arnould, T. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24360 · Cited by 155 · see citing works
Shaping the dynamic mitochondrial network
Lackner, L. L. (2014) · BMC Biology · doi:10.1186/1741-7007-12-35 · Cited by 148 · see citing works
Mitochondrial Dysfunction Contributes to the Pathogenesis of Alzheimer’s Disease
Cabezas-Opazo, F., Vergara-Pulgar, K., Maria Jose Perez, J., Jara, C., Osorio‐Fuentealba, C., & Quintanilla, R. A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/509654 · Cited by 148 · see citing works
Acute exercise remodels mitochondrial membrane interactions in mouse skeletal muscle
Picard, M. A., Gentil, B. J., McManus, M. J., White, K., Louis, K. S., Gartside, S. E., Wallace, D. C., & Turnbull, D. M. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00819.2013 · Cited by 145 · see citing works
Mitochondrial dynamism and heart disease: changing shape and shaping change
Dorn, G. W. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201404575 · Cited by 147 · see citing works
OPA1 and MICOS Regulate mitochondrial crista dynamics and formation
Hu, C., Shu, L., Huang, X., Yu, J., Li, L., Gong, L., Yang, M., Wu, Z., Gao, Z. Y., Zhao, Y., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03152-y · Cited by 142 · see citing works
Exercise training decreases activation of the mitochondrial fission protein dynamin-related protein-1 in insulin-resistant human skeletal muscle
Fealy, C. E., Mulya, A., Lai, N., & Kirwan, J. P. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01064.2013 · Cited by 140 · see citing works
Structural Insights into the Mechanism of Dynamin Superfamily Proteins
Jimah, J. R., & Hinshaw, J. E. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.11.003 · Cited by 134 · see citing works
Hypoxic Regulation of Mitochondrial Metabolism and Mitophagy in Nucleus Pulposus Cells Is Dependent on HIF-1α–BNIP3 Axis
Madhu, V., Boneski, P. K., Silagi, E. S., Qiu, Y., Kurland, I. J., Guntur, A. R., Shapiro, I. M., & Risbud, M. V. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.4019 · Cited by 134 · see citing works
Slower Dynamics and Aged Mitochondria in Sporadic Alzheimer’s Disease
Martín-Maestro, P., Gargini, R., García, E., Perry, G. L., Ávila, J., & García‐Escudero, V. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/9302761 · Cited by 137 · see citing works
Exercise and mitochondrial dynamics: keeping in shape with ROS and AMPK
Trewin, A., Berry, B., & Wojtovich, A. (2018) · Antioxidants · doi:10.3390/antiox7010007 · Cited by 129 · see citing works
Mitoconfusion: Noncanonical Functioning of Dynamism Factors in Static Mitochondria of the Heart
Song, M., & Dorn, G. W. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2014.12.019 · Cited by 127 · see citing works
Perturbation in Mitochondrial Network Dynamics and in Complex I Dependent Cellular Respiration in Schizophrenia
Rosenfeld, M., Brenner-Lavie, H., Gal-Ben-Ari, S., Kavushansky, A., & Ben‐Shachar, D. (2011) · Biological Psychiatry · doi:10.1016/j.biopsych.2011.01.010 · Cited by 132 · see citing works

Molecular mechanism of mitochondrial membrane fusion
Griffin, E. E., Detmer, S. A., & Chan, D. C. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.02.003 · Cited by 73 · see citing works
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 · see citing works
Review Molecular mechanism of mitochondrial membrane fusion
Griffin, E. E., Detmer, S. A., & Chan, D. C. (2006)
New insights into mitochondrial fusion
Zhang, Y., & Chan, D. C. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.01.095 · Cited by 58 · see citing works
Proteolytic Cleavage of Opa1 Stimulates Mitochondrial Inner Membrane Fusion and Couples Fusion to Oxidative Phosphorylation
Mishra, P., Carelli, V., Manfredi, G., & Chan, D. C. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.011 · Cited by 473 · see citing works

Authors: Song, Z., Ghochani, M., McCaffery, J. M., Frey, T. G., & Chan, D. C.
Affiliations: California Institute of Technology (US)
Departments of ‡Physics and
Johns Hopkins University (US)
San Diego State University (US)
ORCID: Song, Zhiyin
McCaffery, J. Michael
Chan, David C.
Venue: Molecular Biology of the Cell
Publisher: American Society for Cell Biology (ASCB)
Published: 2009-08
Volume: 20
Issue: 15
Pages: 3525-3532
ISSN: 1059-1524 (ISSN-L)
1939-4586
DOI: 10.1091/mbc.e09-03-0252
PMC: PMC2719570
OpenAlex: W2164886443
Cited by: 623
References: 38
Citations by year: 2026: 32 · 2025: 45 · 2024: 46 · 2023: 39 · 2022: 62 · 2021: 41 · 2020: 41 · 2019: 35 · 2018: 36 · 2017: 36 · 2016: 31 · 2015: 33 · 2014: 33 · 2013: 38 · 2012: 31
FWCI: 9.79
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Molecular Biology of the Cell (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
CaltechAUTHORS (California Institute of Technology) (submittedVersion, cc-by-nc-sa)
Funders: California Institute of Technology
National Institutes of Health
National Institute of General Medical Sciences (R01GM062967, GM062967)
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 › ATP Synthase and ATPases Research
Keywords: mitochondrial fusion, mitofusins, Mfn1, mitofusin 2, OPA1, prohibitin, autosomal dominant optic atrophy, GTPase
MeSH terms: Animals, Cell Fusion, Cells, Cultured, Fibroblasts, Hybrid Cells, Membrane Fusion, Membrane Proteins, Microscopy, Electron, Polyethylene Glycols, Mice, Knockout, Microscopy, Confocal, GTP Phosphohydrolases, Mitochondrial Proteins, Adaptor Proteins, Signal Transducing, Green Fluorescent Proteins, Mitochondrial Membranes, Mice

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Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion

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