Cited by 734Mitochondrial Function and PathologyAutophagy in Disease and TherapyCell death mechanisms and regulation

The DOI matches its Crossref record; 103 of the 103 references it cites were found in a registry or an index.

Mitochondrial fusion and fission: The fine‐tune balance for cellular homeostasis

Open access

Adebayo, Mary, Singh, Seema, Singh, Ajay Pratap, Dasgupta, Santanu·2021·The FASEB Journal

DOI 10.1096/fj.202100067rPMC PMC8415099

Open this paper in CoChat — free account

Abstract

Mitochondria are highly dynamic, maternally inherited cytoplasmic organelles, which fulfill cellular energy demand through the oxidative phosphorylation system. Besides, they play an active role in calcium and damage‐associated molecular patterns signaling, amino acid, and lipid metabolism, and apoptosis. Thus, the maintenance of mitochondrial integrity and homeostasis is extremely critical, which is achieved through continual fusion and fission. Mitochondrial fusion allows the transfer of gene products between mitochondria for optimal functioning, especially under metabolic and environmental stress. On the other hand, fission is crucial for mitochondrial division and quality control. The imbalance between these two processes is associated with various ailments such as cancer, neurodegenerative and cardiovascular diseases. This review discusses the molecular mechanisms that control mitochondrial fusion and fission and how the disruption of mitochondrial dynamics manifests into various disease conditions.

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

Crossref · 10.1096/fj.202100067r

Cites

103 of 103 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Endothelial Cell Dysfunction and the Pathobiology of Atherosclerosis
Gimbrone, M. A., & García‐Cardeña, G. (2016) · Circulation Research · doi:10.1161/circresaha.115.306301 · Cited by 3,694
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
Mitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002
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
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
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
Mitochondrial Dynamics and Its Involvement in Disease
Chan, D. C. (2020) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-012419-032711 · Cited by 1,416
Mitochondrial dynamics: overview of molecular mechanisms
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397
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
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
PINK1-Phosphorylated Mitofusin 2 Is a Parkin Receptor for Culling Damaged Mitochondria
Chen, Y., & Dorn, G. W. (2013) · Science · doi:10.1126/science.1231031 · Cited by 1,323
Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission.
Taguchi, N., Ishihara, N., Jofuku, A., Oka, T., & Mihara, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607279200 · Cited by 1,226
Fusion and fission: interlinked processes critical for mitochondrial health
Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196
Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation
Rambold, A. S., Kostelecky, B., Elia, N., & Lippincott‐Schwartz, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107402108 · Cited by 1,188
Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808249105 · Cited by 1,129
S-Nitrosylation of Drp1 Mediates β-Amyloid-Related Mitochondrial Fission and Neuronal Injury
Cho, D.-H., Nakamura, T., Fang, J., Cieplak, P., Godzik, A., Gu, Z., & Lipton, S. A. (2009) · Science · doi:10.1126/science.1171091 · Cited by 1,092
Reversible phosphorylation of Drp1 by cyclic AMP‐dependent protein kinase and calcineurin regulates mitochondrial fission and cell death
Cribbs, J. T., & Strack, S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7401062 · Cited by 1,061
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
Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
Ishihara, N., Fujita, Y., Oka, T., & Mihara, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601184 · Cited by 899
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
An Actin-Dependent Step in Mitochondrial Fission Mediated by the ER-Associated Formin INF2
Korobova, F., Ramabhadran, V., & Higgs, H. N. (2013) · Science · doi:10.1126/science.1228360 · Cited by 817
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 796
Mitochondrial dynamics regulates migration and invasion of breast cancer cells
Zhao, J., Zhang, J., Yu, M., Xie, Y., Huang, Y., Wolff, D. W., Abel, P. W., & Tu, Y. (2012) · Oncogene · doi:10.1038/onc.2012.494 · Cited by 783
Erk2 Phosphorylation of Drp1 Promotes Mitochondrial Fission and MAPK-Driven Tumor Growth
Kashatus, J. A., Nascimento, A., Myers, L. J., Sher, A., Byrne, F. L., Hoehn, K. L., Counter, C. M., & Kashatus, D. F. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.002 · Cited by 721
Bioenergetic role of mitochondrial fusion and fission
Westermann, B. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.02.033 · Cited by 687
Endosymbiosis and Eukaryotic Cell Evolution
Archibald, J. M. (2015) · Current Biology · doi:10.1016/j.cub.2015.07.055 · Cited by 654
Mitochondrial dynamics, mitophagy and cardiovascular disease
Vásquez-Trincado, C., García‐Carvajal, I., Pennanen, C., Parra, V., Hill, J. A., Rothermel, B. A., & Lavandero, S. (2015) · The Journal of Physiology · doi:10.1113/jp271301 · Cited by 637
Developmentally Regulated Mitochondrial Fusion Mediated by a Conserved, Novel, Predicted GTPase
Hales, K. G., & Fuller, M. T. (1997) · Cell · doi:10.1016/s0092-8674(00)80319-0 · Cited by 611
Inhibition of mitochondrial fission prevents cell cycle progression in lung cancer
Rehman, J., Zhang, H. J., Tóth, P. T., Zhang, Y., Marsboom, G., Hong, Z., Salgia, R., Husain, A. N., Wietholt, C., & Archer, S. L. (2012) · The FASEB Journal · doi:10.1096/fj.11-196543 · Cited by 610
Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage
Griparić, L., Kanazawa, T., & van der Bliek, A. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704112 · Cited by 486
Mitochondrial dysfunction and mitochondrial dynamics-The cancer connection
Srinivasan, S., Guha, M., Kashina, A., & Avadhani, N. G. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.01.004 · Cited by 452
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
SIRT3 Deacetylates and Activates OPA1 To Regulate Mitochondrial Dynamics during Stress
Samant, S. A., Zhang, H. J., Hong, Z., Pillai, V. B., Sundaresan, N. R., Wolfgeher, D., Archer, S. L., Chan, D. C., & Gupta, M. P. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01483-13 · Cited by 446
Mitochondrial control by DRP1 in brain tumor initiating cells
Xie, Q., Wu, Q., Horbinski, C., Flavahan, W. A., Yang, K., Zhou, W., Dombrowski, S. M., Huang, Z., Fang, X., Shi, Y., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.3960 · Cited by 422
Molecular basis of selective mitochondrial fusion by heterotypic action between OPA1 and cardiolipin
Ban, T., Ishihara, T., Kohno, H., Saita, S., Ichimura, A., Maenaka, K., Oka, T., Mihara, K., & Ishihara, N. (2017) · Nature Cell Biology · doi:10.1038/ncb3560 · Cited by 410
MFN2 mutation distribution and genotype/phenotype correlation in Charcot-Marie-Tooth type 2
Verhoeven, K. (2006) · Brain · doi:10.1093/brain/awl126 · Cited by 408
Increased mitochondrial fission promotes autophagy and hepatocellular carcinoma cell survival through the ROS-modulated coordinated regulation of the NFKB and TP53 pathways
Huang, Q., Zhan, L., Cao, H., Li, J., Lyu, Y., Guo, X., Zhang, J., Ji, L., Ren, T., An, J., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1166318 · Cited by 403
Parkin Ubiquitinates Drp1 for Proteasome-dependent Degradation
Wang, H., Song, P., Du, L., Tian, W., Yue, W., Liu, M., Li, D., Wang, B., Zhu, Y., Cao, C., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.144238 · Cited by 392
Metformin suppresses diabetes-accelerated atherosclerosis via the inhibition of drp1-mediated mitochondrial fission
Wang, Q., Zhang, M., Torres, G., Wu, S., Ouyang, C., Xie, Z., & Zou, M.-H. (2017) · Diabetes · doi:10.2337/db16-0915 · Cited by 370
Mitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity
Bertholet, A. M., Delerue, T., Millet, A. M., Moulis, M. F., David, C., Daloyau, M., Arnauné-Pelloquin, L., Davezac, N., Mils, V., Miquel, M. C., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.011 · Cited by 363
INF2-mediated actin polymerization at the ER stimulates mitochondrial calcium uptake, inner membrane constriction, and division
Chakrabarti, R., Ji, W.-K., Stan, R. V., de Juan Sanz, J., Ryan, T. A., & Higgs, H. N. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201709111 · Cited by 349
A mitochondria-anchored isoform of the actin-nucleating spire protein regulates mitochondrial division
Manor, U., Bartholomew, S. R., Golani, G., Christenson, E. T., Kozlov, M. M., Higgs, H. N., Spudich, J. A., & Lippincott‐Schwartz, J. (2015) · eLife · doi:10.7554/elife.08828 · Cited by 342
MAPL SUMOylation of Drp1 Stabilizes an ER/Mitochondrial Platform Required for Cell Death
Prudent, J., Zunino, R., Sugiura, A., Mattie, S., Shore, G. C., & McBride, H. M. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.001 · Cited by 335
Stress-Induced Phosphorylation and Proteasomal Degradation of Mitofusin 2 Facilitates Mitochondrial Fragmentation and Apoptosis
Leboucher, G. P., Tsai, Y. C., Yang, M., Shaw, K. C., Zhou, M., Veenstra, T. D., Glickman, M. H., & Weissman, A. M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.041 · Cited by 334
MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion
Cao, Y.-L., Meng, S., Chen, Y., Feng, J.-X., Gu, D.-D., Yu, B., Li, Y.-J., Yang, J.-Y., Liao, S., Chan, D. C., et al. (2017) · Nature · doi:10.1038/nature21077 · Cited by 326
Abnormal mitochondrial dynamics and neurodegenerative diseases
Su, B., Wang, X., Zheng, L., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.013 · Cited by 301
Dominant optic atrophy
Lenaers, G., Hamel, C., Delettre, C., Amati‐Bonneau, P., Procaccio, V., Bonneau, D., Reynier, P., & Miléa, D. (2012) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-7-46 · Cited by 299
Abnormal Mitochondrial Morphology in Sporadic Parkinson's and Alzheimer's Disease Cybrid Cell Lines
Trimmer, P. A., Swerdlow, R. H., Parks, J. K., Keeney, P. M., Bennett, J. P., Miller, S. W., Davis, R. E., & Parker, W. D. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7333 · Cited by 296
Recent advances into the understanding of mitochondrial fission
Elgass, K., Pakay, J. L., Ryan, M. T., & Palmer, C. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.002 · Cited by 274
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
Dynamin-related protein 1 has membrane constricting and severing abilities sufficient for mitochondrial and peroxisomal fission
Kamerkar, S. C., Kraus, F., Sharpe, A. J., Pucadyil, T. J., & Ryan, M. T. (2018) · Nature Communications · doi:10.1038/s41467-018-07543-w · Cited by 252
Extracellular Regulated Kinase Phosphorylates Mitofusin 1 to Control Mitochondrial Morphology and Apoptosis
Pyakurel, A., Savoia, C., Hess, D., & Scorrano, L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.021 · Cited by 244
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 239
The HMGB1/RAGE inflammatory pathway promotes pancreatic tumor growth by regulating mitochondrial bioenergetics
Kang, R., Tang, D., Schapiro, N. E., Loux, T., Livesey, K. M., Billiar, T. R., Wang, H., Houten, B. V., Lotze, M. T., & Zeh, H. J. (2013) · Oncogene · doi:10.1038/onc.2012.631 · Cited by 233
OPA1 alternate splicing uncouples an evolutionary conserved function in mitochondrial fusion from a vertebrate restricted function in apoptosis
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
MFN2 mutations cause severe phenotypes in most patients with CMT2A
Feely, S. M. E., Laurá, M., Siskind, C. E., Sottile, S. L., Davis, M. B., Gibbons, V. S., Reilly, M. M., & Shy, M. E. (2011) · Neurology · doi:10.1212/wnl.0b013e31821a441e · Cited by 222
Transient assembly of F-actin on the outer mitochondrial membrane contributes to mitochondrial fission
Li, S., Xu, S., Roelofs, B. A., Boyman, L., Lederer, W. J., Sesaki, H., & Karbowski, M. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201404050 · Cited by 214
Modulation of Dynamin-related Protein 1 (DRP1) Function by Increased O-linked-β-N-acetylglucosamine Modification (O-GlcNAc) in Cardiac Myocytes
Gawlowski, T., Suárez, J., Scott, B. T., Torres‐Gonzalez, M., Wang, H., Schwappacher, R., Han, X., Yates, J. R., Hoshijima, M., & DILLMANN, W. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.390682 · Cited by 214
Mitochondrial division/mitophagy inhibitor (Mdivi) Ameliorates Pressure Overload Induced Heart Failure
Givvimani, S., Munjal, C., Tyagi, N., Sen, U., Metreveli, N. S., & Tyagi, S. C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032388 · Cited by 203
MFN1-dependent alteration of mitochondrial dynamics drives hepatocellular carcinoma metastasis by glucose metabolic reprogramming
Zhang, Z., Li, T., Chen, M., Xu, D., Zhu, Y., Hu, B., Lin, Z., Pan, J.-J., Wang, X., Wu, C., et al. (2019) · British Journal of Cancer · doi:10.1038/s41416-019-0658-4 · Cited by 198
Mitochondria mass is low in mouse substantia nigra dopamine neurons: Implications for Parkinson's disease
Liang, C., Wang, T. T., Luby‐Phelps, K., & German, D. C. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2006.08.015 · Cited by 190
Clinical and electrophysiologic features of CMT2A with mutations in the mitofusin 2 gene
Lawson, V. H., Graham, B. V., & Flanigan, K. M. (2005) · Neurology · doi:10.1212/01.wnl.0000168898.76071.70 · Cited by 183
Structures of human mitofusin 1 provide insight into mitochondrial tethering
Qi, Y., Yan, L., Yu, C., Guo, X., Zhou, X., Hu, X., Huang, X., Rao, Z., Lou, Z., & Hu, J. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201609019 · Cited by 180
Mitochondrial fusion exploits a therapeutic vulnerability of pancreatic cancer
Yu, M., Nguyen, N. D., Huang, Y., Lin, D., Fujimoto, T. N., Molkentine, J. M., Deorukhkar, A., Kang, Y., Lucas, F. A. S., Fernandes, C. J., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.126915 · Cited by 176
Two Forms of Opa1 Cooperate to Complete Fusion of the Mitochondrial Inner-Membrane
Ge, Y., Shi, X., Boopathy, S., McDonald, J., Smith, A. W., & Chao, L. H. (2020) · eLife · doi:10.7554/elife.50973 · Cited by 174
Mitochondrial fission induced by platelet-derived growth factor regulates vascular smooth muscle cell bioenergetics and cell proliferation
Salabei, J. K., & Hill, B. G. (2013) · Redox Biology · doi:10.1016/j.redox.2013.10.011 · Cited by 169
A dimeric equilibrium intermediate nucleates Drp1 reassembly on mitochondrial membranes for fission
Macdonald, P. J., Stepanyants, N., Mehrotra, N., Mears, J. A., Qi, X., Sesaki, H., & Ramachandran, R. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-02-0728 · Cited by 169
A new mitofusin topology places the redox-regulated C terminus in the mitochondrial intermembrane space
Mattie, S., Riemer, J., Wideman, J. G., & McBride, H. M. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201611194 · Cited by 169
The C. elegans Opa1 Homologue EAT-3 Is Essential for Resistance to Free Radicals
Kanazawa, T., Zappaterra, M., Hasegawa, A., Wright, A. P., Newman-Smith, E. D., BUTTLE, K. F., McDonald, K. L., Mannella, C. A., & van der Bliek, A. M. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000022 · Cited by 164
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
HMGB1 promotes ERK-mediated mitochondrial Drp1 phosphorylation for chemoresistance through RAGE in colorectal cancer
Huang, C.-Y., Chiang, S., Chen, W. T., Ke, T., Chen, T.-W., You, Y., Lin, C., Chao, K. S. C., & Huang, C. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1019-6 · Cited by 155
Hindlimb gait defects due to motor axon loss and reduced distal muscles in a transgenic mouse model of Charcot–Marie–Tooth type 2A
Detmer, S. A., Velde, C. V., Cleveland, D. W., & Chan, D. C. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm314 · Cited by 148
Involvement of Drp1 in hypoxia-induced migration of human glioblastoma U251 cells
Wan, Y., Zhang, J., Yang, Z., Jiang, L., WEI, Y.-F., Lai, Q., WANG, J.-B., XIN, H.-B., & Han, X. (2014) · Oncology Reports · doi:10.3892/or.2014.3235 · Cited by 144
MFN2-related neuropathies: Clinical features, molecular pathogenesis and therapeutic perspectives
Stuppia, G., Rizzo, F., Riboldi, G. M., Bo, R. D., Nizzardo, M., Simone, C., Comi, G. P., Bresolin, N., & Corti, S. P. (2015) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2015.05.033 · Cited by 138
High frequency of mitochondrial complex I mutations in Parkinson’s disease and aging
Smigrodzki, R. M., Parks, J. K., & Parker, W. D. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.020 · Cited by 138
MFN1 deacetylation activates adaptive mitochondrial fusion and protects metabolically challenged mitochondria
Lee, J., Kapur, M., Li, M., Choi, M., Choi, S., Kim, H.-J., Kim, I., Lee, E. J., Taylor, J. P., & Yao, T. (2014) · Journal of Cell Science · doi:10.1242/jcs.157321 · Cited by 134
Charcot-Marie-Tooth Disease Type 2A
Bombelli, F., Stojkovic, T., Dubourg, O., Echaniz‐Laguna, A., Tardieu, S., Larcher, K., Amati‐Bonneau, P., Latour, P., Vignal, O., Cazeneuve, C., et al. (2014) · JAMA Neurology · doi:10.1001/jamaneurol.2014.629 · Cited by 132
Mitochondrial dynamics and cancer
Maycotte, P., Marín‐Hernández, Á., Goyri-Aguirre, M., Anaya-Ruı́z, M., Reyes‐Leyva, J., & Cortés-Hernández, P. (2017) · Tumor Biology · doi:10.1177/1010428317698391 · Cited by 125
Mitochondrial Fusion Via OPA1 and MFN1 Supports Liver Tumor Cell Metabolism and Growth
Li, M., Wang, L., Wang, Y., Zhang, S., Zhou, G., Lieshout, R., Ma, B., Liu, J., Qu, C., Verstegen, M. M. A., et al. (2020) · Cells · doi:10.3390/cells9010121 · Cited by 124
The Impact of Mitochondrial Fusion and Fission Modulation in Sporadic Parkinson’s Disease
Santos, D., Esteves, A. R., Silva, D. F., Januário, C., & Cardoso, S. M. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8893-4 · Cited by 117
Expression of mitofusin 2R94Q in a transgenic mouse leads to Charcot–Marie–Tooth neuropathy type 2A
Cartoni, R., Arnaud, E., Médard, J., Poirot, O., Courvoisier, D. S., Chrast, R., & Martinou, J. (2010) · Brain · doi:10.1093/brain/awq082 · Cited by 115
The rescue of microtubule-dependent traffic recovers mitochondrial function in Parkinson's disease
Esteves, A. R., Gozes, I., & Cardoso, S. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.10.003 · Cited by 110
OPA1 cleavage depends on decreased mitochondrial ATP level and bivalent metals
Baricault, L., Ségui, B., Guégand, L., Olichon, A., Valette, A., Larminat, F., & Lenaers, G. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.08.008 · Cited by 109
Increased mitochondrial fission and neuronal dysfunction in Huntington's disease: implications for molecular inhibitors of excessive mitochondrial fission
Reddy, P. H. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.03.020 · Cited by 109
The role of mitochondrial dynamics in human cancers.
Ma, Y., Wang, L., & Jia, R. (2020) · PubMed Central · Cited by 99
OPA1 Deficiency Associated with Increased Autophagy in Retinal Ganglion Cells in a Murine Model of Dominant Optic Atrophy
White, K., Davies, V. J., Hogan, V. E., Piechota, M. J., Nichols, P. P., Turnbull, D. M., & Votruba, M. (2009) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.08-2913 · Cited by 98
Expression of mitochondrial fusion–fission proteins during post-infarction remodeling: the effect of NHE-1 inhibition
Javadov, S. A., Rajapurohitam, V., Kilić, A., Hunter, J. C., Zeidan, A., Faruq, N. S., Escobales, N., & Karmazyn, M. (2010) · Basic Research in Cardiology · doi:10.1007/s00395-010-0122-3 · Cited by 93
Mitochondrial metabolism in Parkinson's disease impairs quality control autophagy by hampering microtubule-dependent traffic
Arduíno, D. M., Esteves, A. R., Cortes, L., Silva, D. F., Patel, B., Grazina, M. M., Swerdlow, R. H., Oliveira, C. R., & Cardoso, S. M. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds309 · Cited by 87
Cofilin1-dependent actin dynamics control DRP1-mediated mitochondrial fission
Rehklau, K., Hoffmann, L., Gurniak, C. B., Ott, M., Witke, W., Scorrano, L., Culmsee, C., & Rust, M. B. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.448 · Cited by 86
Positive feedback loop between mitochondrial fission and Notch signaling promotes survivin-mediated survival of TNBC cells
Chen, L., Zhang, J., Lyu, Z., Chen, Y., Ji, X., Cao, H., Jin, M., Zhu, J., Jin, Y., Ling, R., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1083-y · Cited by 85
Enhanced mitochondrial fission suppresses signaling and metastasis in triple-negative breast cancer
Humphries, B. A., Cutter, A. C., Buschhaus, J. M., Chen, Y., Qyli, T., Palagama, D. S. W., Eckley, S. S., Robison, T. H., Bevoor, A. S., Chiang, B., et al. (2020) · Breast Cancer Research · doi:10.1186/s13058-020-01301-x · Cited by 84
Microtubule depolymerization potentiates alpha-synuclein oligomerization
Esteves, A. R. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/neuro.24.005.2009 · Cited by 71
Metabolic Stress-Induced Phosphorylation of KAP1 Ser473 Blocks Mitochondrial Fusion in Breast Cancer Cells
Cheng, C.-T., Kuo, C., Ouyang, C., Li, C., Chung, Y., Chan, D. C., Kung, H.-J., & Ann, D. K. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2921 · Cited by 66
The role of dynamin-related protein 1 in cancer growth: a promising therapeutic target?
Qian, W., Wang, J., & Houten, B. V. (2013) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.823160 · Cited by 62
Mitochondrial Fusion/Fission, Transport and Autophagy in Parkinson's Disease: When Mitochondria Get Nasty
Arduíno, D. M., Esteves, A. R., & Cardoso, S. M. (2011) · Parkinson s Disease · doi:10.4061/2011/767230 · Cited by 61
Improved Locus-Specific Database forOPA1Mutations Allows Inclusion of Advanced Clinical Data
Ferré, M., Caignard, A., Miléa, D., Leruez, S., Cassereau, J., Chevrollier, A., Amati‐Bonneau, P., Verny, C., Bonneau, D., Procaccio, V., et al. (2014) · Human Mutation · doi:10.1002/humu.22703 · Cited by 54
Disruption of mitochondrial dynamics increases stress resistance through activation of multiple stress response pathways
Machiela, E., Liontis, T., Dues, D. J., Rudich, P. D., Traa, A., Wyman, L., Kaufman, C., Cooper, J. F., Lew, L., Nadarajan, S., et al. (2020) · The FASEB Journal · doi:10.1096/fj.201903235r · Cited by 54
Mitochondrial Reprogramming Regulates Breast Cancer Progression
Kannan, A., Wells, R. B., Sivakumar, S., Komatsu, S., Singh, K. P., Samten, B., Philley, J. V., Sauter, E. R., Ikebe, M., Idell, S., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-2456 · Cited by 53
Self-citation
Mice Hemizygous for a Pathogenic Mitofusin-2 Allele Exhibit Hind Limb/Foot Gait Deficits and Phenotypic Perturbations in Nerve and Muscle
Bannerman, P. G. C., Burns, T., Xu, J., Miers, L. A., & Pleasure, D. (2016) · PLoS ONE · doi:10.1371/journal.pone.0167573 · Cited by 38
Mitochondrial fission and fusion
Patrushev, M. V., Mazunin, I., Vinogradova, E. N., & Kamenski, P. A. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915110061 · Cited by 31
Ropivacaine Prevents the Activation of the NLRP3 Inflammasome Caused by High Glucose in HUVECs
Huang, X., Jiang, J., Huang, L., Ren, Q., Gao, X., & Yu, S. (2020) · ACS Omega · doi:10.1021/acsomega.0c03143 · Cited by 3
Correction: Mice Hemizygous for a Pathogenic Mitofusin-2 Allele Exhibit Hind Limb/Foot Gait Deficits and Phenotypic Perturbations in Nerve and Muscle
Bannerman, P. G. C., Burns, T., Xu, J., Miers, L. A., & Pleasure, D. (2018) · PLoS ONE · doi:10.1371/journal.pone.0204536 · Cited by 1

Sorted by citations

Inflammation and aging: signaling pathways and intervention therapies
Li, X., Li, C., Zhang, W., Wang, Y., Qian, P., & Huang, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01502-8 · Cited by 1,443
“Oxidative stress leads to oxidative damage to biomolecules (especially DNA),(201) causing endogenous damageassociated molecular patterns (DAMPs) production and cytokine release in the organism.(202,203) Cytokines activate downstream signaling pathways of pattern recognition receptors,(203) causing systemic chronic inf…”
Background
Mitochondria: It is all about energy
Casanova, A., Wevers, A., Ledesma, S. N., & Pruimboom, L. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1114231 · Cited by 350
Emerging insights into the pathogenesis and therapeutic strategies for vascular endothelial injury-associated diseases: focus on mitochondrial dysfunction
Pang, B., Dong, G., Pang, T., Sun, X., Liu, X., Nie, Y., & Chang, X. (2024) · Angiogenesis · doi:10.1007/s10456-024-09938-4 · Cited by 282
Mitochondrial Glutathione in Cellular Redox Homeostasis and Disease Manifestation
Chen, T., Wang, H., Chang, C.-J., & Lee, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25021314 · Cited by 250
“Unlike mitochondrial fission, which promotes apoptosis, mitochondrial fusion occurs via the interferon-responsive cGAMP interactor 1–mitochondrial fusion 1/2 (MFN1/2) pathway [116].”
Background
Mitochondrial dynamics maintain muscle stem cell regenerative competence throughout adult life by regulating metabolism and mitophagy
Hong, X., Isern, J., Campanario, S., Perdiguero, E., Ramírez-Pardo, I., Segalés, J., Hernansanz-Agustín, P., Curtabbi, A., Deryagin, O., Pollán, A., et al. (2022) · Cell stem cell · doi:10.1016/j.stem.2022.07.009 · Cited by 213

See all 734

Authors: Adebayo, M., Singh, S., Singh, A. P., & Dasgupta, S.
Affiliations: USA Mitchell Cancer Institute (US)
Corresponding author: Singh, Ajay Pratap
Dasgupta, Santanu
ORCID: Singh, Seema
Dasgupta, Santanu
Venue: The FASEB Journal
Publisher: Wiley
Published: 2021-05-28
Volume: 35
Issue: 6
Pages: e21620-e21620
ISSN: 0892-6638 (ISSN-L)
1530-6860
DOI: 10.1096/fj.202100067r
PMC: PMC8415099
OpenAlex: W3164775823
Cited by: 733
References: 103
Citations by year: 2026: 189 · 2025: 235 · 2024: 183 · 2023: 83 · 2022: 38 · 2021: 4
FWCI: 8.11
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: The FASEB Journal (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (CA185490, CA224306, CA204801, CA231925)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
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 homeostasis, mitochondrial quality control, mitochondrial division, oxidative phosphorylation, calcium signaling, damage-associated molecular patterns, apoptosis, mitochondrial metabolism, neurodegenerative diseases, cardiovascular disease, cancer
MeSH terms: Animals, Homeostasis, Humans, Mitochondria, Mitochondrial Dynamics

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

Mitochondrial fusion and fission: The fine‐tune balance for cellular homeostasis

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks