The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Mitochondrial dynamics-fusion, fission, movement, and mitophagy-in neurodegenerative diseases
Open accessAbstract
Neurons are metabolically active cells with high energy demands at locations distant from the cell body. As a result, these cells are particularly dependent on mitochondrial function, as reflected by the observation that diseases of mitochondrial dysfunction often have a neurodegenerative component. Recent discoveries have highlighted that neurons are reliant particularly on the dynamic properties of mitochondria. Mitochondria are dynamic organelles by several criteria. They engage in repeated cycles of fusion and fission, which serve to intermix the lipids and contents of a population of mitochondria. In addition, mitochondria are actively recruited to subcellular sites, such as the axonal and dendritic processes of neurons. Finally, the quality of a mitochondrial population is maintained through mitophagy, a form of autophagy in which defective mitochondria are selectively degraded. We review the general features of mitochondrial dynamics, incorporating recent findings on mitochondrial fusion, fission, transport and mitophagy. Defects in these key features are associated with neurodegenerative disease. Charcot-Marie-Tooth type 2A, a peripheral neuropathy, and dominant optic atrophy, an inherited optic neuropathy, result from a primary deficiency of mitochondrial fusion. Moreover, several major neurodegenerative diseases--including Parkinson's, Alzheimer's and Huntington's disease--involve disruption of mitochondrial dynamics. Remarkably, in several disease models, the manipulation of mitochondrial fusion or fission can partially rescue disease phenotypes. We review how mitochondrial dynamics is altered in these neurodegenerative diseases and discuss the reciprocal interactions between mitochondrial fusion, fission, transport and mitophagy.
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.
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
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601
Self-citationMitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
Clark, I. E., Dodson, M. W., Jiang, C., Cao, J. H., Huh, J. R., Seol, J. H., Yoo, S. J., Hay, B. A., & Guo, M. (2006) · Nature · doi:10.1038/nature04779 · Cited by 1,788
Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
Park, J., Lee, S. B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J.-M., et al. (2006) · Nature · doi:10.1038/nature04788 · Cited by 1,705
OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion
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
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 · cited 1×
“neuropathy affecting sensory and motor neurons of the distal extremities (8).”
BackgroundSelective degradation of mitochondria by mitophagy
Kim, I., Rodriguez-Enriquez, S., & Lemasters, J. J. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.034 · Cited by 1,558
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 · cited 8×
“Potential answers include differential expression patterns between Mfn2 versus OPA1, functional differences between OPA1 (11) and Mfn2 (12), differences in an outer membrane fusion defect versus an inner membrane fusion defect (4) and redundancy between Mfn1 and Mfn2 (6,13).”
BackgroundInfluentialSelf-citation
Cited by
Mitochondrial dynamics in health and disease: mechanisms and potential targets
Chen, W., Zhao, H., & Li, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01547-9 · Cited by 1,306
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
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
Mitochondrial Dysfunction and Oxidative Stress in Alzheimer’s Disease
Misrani, A., Tabassum, S., & Yang, L. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.617588 · Cited by 654
Mitochondrial optic neuropathies—Disease mechanisms and therapeutic strategies
Yu-Wai-Man, P., Griffiths, P. G., & Chinnery, P. F. (2011) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2010.11.002 · Cited by 633
Mitophagy-dependent necroptosis contributes to the pathogenesis of COPD
Mizumura, K., Cloonan, S. M., Nakahira, K., Bhashyam, A. R., Cervo, M., Kitada, T., Glass, K., Owen, C. A., Mahmood, A., Washko, G. R., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci74985 · Cited by 611
MAM (mitochondria-associated membranes) in mammalian cells: Lipids and beyond
Vance, J. E. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.11.014 · Cited by 625
Vitamin B 3 modulates mitochondrial vulnerability and prevents glaucoma in aged mice
Williams, P. A., Harder, J. M., Foxworth, N. E., Cochran, K. E., Philip, V. M., Porciatti, V., Smithies, O., & John, S. W. M. (2017) · Science · doi:10.1126/science.aal0092 · Cited by 617
Mitochondria: The Next (Neurode)Generation
Schon, E. A., & Przedborski, S. (2011) · Neuron · doi:10.1016/j.neuron.2011.06.003 · Cited by 568
Differential responses to lithium in hyperexcitable neurons from patients with bipolar disorder
Study, T. P. O. B. D., Mertens, J., Wang, Q.-W., Kim, Y., Yu, D. X., Pham, S., Yang, B., Zheng, Y., Diffenderfer, K. E., Zhang, J., et al. (2015) · Nature · doi:10.1038/nature15526 · Cited by 562
New insights into the role of mitochondria in aging: mitochondrial dynamics and more
Seo, A. Y., Joseph, A.-M., Dutta, D., Hwang, J. C. Y., Aris, J. P., & Leeuwenburgh, C. (2010) · Journal of Cell Science · doi:10.1242/jcs.070490 · Cited by 522
Ashrafi, G., Schlehe, J. S., LaVoie, M. J., & Schwarz, T. L. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201401070 · Cited by 502
“The involvement of PINK1 and Par kin in regulation of mitochondrial dynamics further supports the classification of PD as a mitochondrial disease (Chen and Chan, 2009; Wang et al., 2011).”
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
Mitophagy: An Emerging Role in Aging and Age-Associated Diseases
Chen, G., Kroemer, G., & Kepp, O. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00200 · Cited by 359
Dysfunctional autophagy in RPE, a contributing factor in age-related macular degeneration
Golestaneh, N., Chu, Y., Xiao, Y.-Y., Stoleru, G. L., & Theos, A. C. (2017) · Cell Death & Disease · doi:10.1038/cddis.2016.453 · Cited by 357
Cooperative and independent roles of the Drp1 adaptors Mff, MiD49 and MiD51 in mitochondrial fission
Osellame, L. D., Singh, A. P., Stroud, D. A., Palmer, C. S., Stojanovski, D., Ramachandran, R., & Ryan, M. T. (2016) · Journal of Cell Science · doi:10.1242/jcs.185165 · Cited by 336
ATG12 Conjugation to ATG3 Regulates Mitochondrial Homeostasis and Cell Death
Radoshevich, L., Murrow, L., Chen, N., Fernandez, E., Roy, S., Fung, C., & Debnath, J. (2010) · Cell · doi:10.1016/j.cell.2010.07.018 · Cited by 290
Quirós, P. M., Ramsay, A. J., Sala, D., Fernández‐Vizarra, E., Rodríguez, F., Peinado, J. R., Fernández‐García, M. S., Vega, J. A., Enríquez, J. A., Zorzano, A., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.70 · Cited by 269
Lewis, T. L., Kwon, S.-K., Lee, A., Shaw, R., & Polleux, F. (2018) · Nature Communications · doi:10.1038/s41467-018-07416-2 · Cited by 260
The hallmarks of fibroblast ageing
Tigges, J., Krutmann, J., Fritsche, E., Haendeler, J., Schaal, H., Fischer, J. W., Kalfalah, F., Reinke, H., Reifenberger, G., Stühler, K., et al. (2014) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2014.03.004 · Cited by 250
Abnormalities of Mitochondrial Dynamics in Neurodegenerative Diseases
Gao, J., Wang, L., Liu, J., Xie, F., Su, B., & Wang, X. (2017) · Antioxidants · doi:10.3390/antiox6020025 · Cited by 250
Chen, Y., & Sheng, Z.-H. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201302040 · Cited by 250
Computational classification of mitochondrial shapes reflects stress and redox state
Ahmad, T., Aggarwal, K., Pattnaik, B., Mukherjee, S., Sethi, T., Tiwari, B. K., Kumar, M., Micheal, A., Mabalirajan, U., Ghosh, B., et al. (2013) · Cell Death & Disease · doi:10.1038/cddis.2012.213 · Cited by 233
The Association of Tau With Mitochondrial Dysfunction in Alzheimer’s Disease
Cheng, Y., & Bai, F. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00163 · Cited by 239
Soluble forms of tau are toxic in Alzheimer's disease
Kopeikina, K., Hyman, B., & Spires-Jones, T. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0032-y · Cited by 232
The Interplay of Axonal Energy Homeostasis and Mitochondrial Trafficking and Anchoring
Sheng, Z.-H. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.01.005 · Cited by 221
Circadian rhythms in mitochondrial respiration
de Goede, P., Wefers, J., Brombacher, E. C., Schrauwen, P., & Kalsbeek, A. (2018) · Journal of Molecular Endocrinology · doi:10.1530/jme-17-0196 · Cited by 211
Loss of O -GlcNAc glycosylation in forebrain excitatory neurons induces neurodegeneration
Wang, A. C., Jensen, E. H., Rexach, J. E., Vinters, H. V., & Hsieh-Wilson, L. C. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606899113 · Cited by 211
Goetzman, E. S., & Prochownik, E. V. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00129 · Cited by 199
Mitochondrial abnormalities in temporal lobe of autistic brain
Tang, G., Gutierrez Rios, P., Kuo, S.-H., Akman, H. O., Rosoklija, G., Tanji, K., Dwork, A., Schon, E. A., DiMauro, S., Goldman, J., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.01.006 · Cited by 194
DeBalsi, K. L., Hoff, K. E., & Copeland, W. C. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.006 · Cited by 180
Das, S., Mitrovsky, G., Vasanthi, H. R., & Das, D. K. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/345105 · Cited by 173
RetractedAberrant protein S-nitrosylation contributes to the pathophysiology of neurodegenerative diseases
Nakamura, T., Prikhodko, O. A., Pirie, E., Nagar, S., Akhtar, M. W., Oh, C.-K., McKercher, S. R., Ambasudhan, R., Okamoto, S.-I., & Lipton, S. A. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.03.017 · Cited by 165
Hoitzing, H., Johnston, I. G., & Jones, N. S. (2015) · BioEssays · doi:10.1002/bies.201400188 · Cited by 159
Altered Mitochondrial Dynamics and TBI Pathophysiology
Fischer, T. D., Hylin, M. J., Zhao, J., Moore, A. N., Waxham, M. N., & Dash, P. K. (2016) · Frontiers in Systems Neuroscience · doi:10.3389/fnsys.2016.00029 · Cited by 160
Koltai, E., Hart, N., Taylor, A. W., Goto, S., Ngo, J. K., Davies, K. J. A., & Radak, Z. (2012) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00337.2011 · Cited by 152
Xie, Y., Zhou, B., Lin, M.-Y., Wang, S., Foust, K. D., & Sheng, Z.-H. (2015) · Neuron · doi:10.1016/j.neuron.2015.06.026 · Cited by 149
Impaired Mitochondrial Dynamics and Bioenergetics in Diabetic Skeletal Muscle
Liu, R., Jin, P., LiqunYu, Wang, Y., Han, L., Shi, T., & Li, X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092810 · Cited by 146
Silva, D. F., Selfridge, J. E., Lu, J., E, L., Roy, N., Hutfles, L., Burns, J. M., Michaelis, E. K., Yan, S., Cardoso, S. M., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt247 · Cited by 133
Bernhardt, D., Müller, M., Reichert, A. S., & Osiewacz, H. D. (2015) · Scientific Reports · doi:10.1038/srep07885 · Cited by 125
Frye, R. E. (2015) · Epilepsy & Behavior · doi:10.1016/j.yebeh.2014.08.134 · Cited by 117
Wang, B., Cai, Z., Tao, K., Zeng, W., Lu, F., Yang, R., Feng, D., Gao, G., & Yang, Q. (2016) · Autophagy · doi:10.1080/15548627.2016.1179401 · Cited by 107
Physical Exercise and Brain Mitochondrial Fitness: The Possible Role Against Alzheimer's Disease
Bernardo, T. C., Marques‐Aleixo, I., Beleza, J., Oliveira, P. J., Ascensão, A., & Magalhães, J. (2016) · Brain Pathology · doi:10.1111/bpa.12403 · Cited by 108
van Hameren, G., Campbell, G., Deck, M., Berthelot, J., Gautier, B., Quintana, P., Chrast, R., & Tricaud, N. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0740-4 · Cited by 83
Mitofusin 1 and optic atrophy 1 shift metabolism to mitochondrial respiration during aging.
Son, J. M., Sarsour, E. H., Kakkerla Balaraju, A., Fussell, J., Kalen, A. L., Wagner, B. A., Buettner, G. R., & Goswami, P. C. (2017) · Aging Cell · doi:10.1111/acel.12649 · Cited by 71
Impact of Tau on Neurovascular Pathology in Alzheimer's Disease
Canepa, E., & Fossati, S. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.573324 · Cited by 67
Biochemical analysis of human POLG2 variants associated with mitochondrial disease
Young, M. J., Longley, M. J., Li, F.-Y., Kasiviswanathan, R., Wong, L.-J., & Copeland, W. C. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr209 · Cited by 66
Mitochondrial Dynamics and Parkinson's Disease: Focus on Parkin
Lim, K.-L., Ng, X.-H., Grace, L. G.-Y., & Yao, T.-P. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4105 · Cited by 64
Casinelli, G., LaRosa, J., Sharma, M., Cherok, E., Banerjee, S., Branca, M., Edmunds, L., Wang, Y., Sims-Lucas, S., Churley, L., et al. (2016) · Cell Death Discovery · doi:10.1038/cddiscovery.2016.82 · Cited by 52
Potential biomarkers to follow the progression and treatment response of Huntington’s disease
Disatnik, M.-H., Joshi, A. U., Saw, N. L., Shamloo, M., Leavitt, B. R., Qi, X., & Mochly-Rosen, D. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20160776 · Cited by 58
Liu, Q., Wang, X., Hu, Y., Zhao, J.-N., Huang, C.-H., Li, T., Zhang, B.-G., He, Y., Wu, Y.-Q., Zhang, Z.-J., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102697 · Cited by 58
Risks of cognitive detriments after low dose heavy ion and proton exposures
Cucinotta, F. A., & Cacao, E. (2019) · International Journal of Radiation Biology · doi:10.1080/09553002.2019.1623427 · Cited by 58
Deheshi, S., Dabiri, B., Fan, S., Tsang, M., & Rintoul, G. L. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13090 · Cited by 52
Mitochondrial dynamics in aging and disease
Bereiter-Hahn, J. (2014) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-394625-6.00004-0 · Cited by 48
Novel subcellular localization for α-synuclein: possible functional consequences
Guardia-Laguarta, C., Area-Gomez, E., Schon, E. A., & Przedborski, S. (2015) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2015.00017 · Cited by 44
H. Swerdlow, R. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211798072535 · Cited by 35
Age-Dependent Behavioral and Metabolic Assessment of AppNL−G−F/NL−G−F Knock-in (KI) Mice
Wang, S., Ichinomiya, T., Savchenko, P., Devulapalli, S., Wang, D., Beltz, G., Saito, T., Saido, T. C., Wagner, S. L., Patel, H. H., et al. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.909989 · Cited by 23
Recent trends of natural based therapeutics for mitochondria targeting in Alzheimer’s disease
Dhiman, A., Handa, M., Ruwali, M., Singh, D. P., Kesharwani, P., & Shukla, R. (2022) · Mitochondrion · doi:10.1016/j.mito.2022.03.006 · Cited by 21
Shin, Y. S., Ryall, J. G., Britto, J. M., Lau, C. L., Devenish, R. J., Nagley, P., & Beart, P. M. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14667 · Cited by 13
Breaking up is hard to do: RalA, mitochondrial fission and cancer
Kashatus, D. F., & Counter, C. M. (2011) · Small GTPases · doi:10.4161/sgtp.18284 · Cited by 12
Lys716 in the transmembrane domain of yeast mitofusin Fzo1 modulates anchoring and fusion
Versini, R., Baaden, M., Cavellini, L., Cohen, M. M., Taly, A., & Fuchs, P. F. J. (2024) · Structure · doi:10.1016/j.str.2024.08.017 · Cited by 4
Metadata
- Authors
- Chen, H., & Chan, D. C.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2009-10-06
- Volume
- 18
- Issue
- R2
- Pages
- R169-R176
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2105043890
- Cited by
- 1,458
- References
- 31
- FWCI
- 30.37
- Type
- journal article
- Language
- en
- Open access
- hybrid
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.