Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin
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To minimize oxidative damage to the cell, malfunctioning mitochondria need to be removed by mitophagy. In neuronal axons, mitochondrial damage may occur in distal regions, far from the soma where most lysosomal degradation is thought to occur. In this paper, we report that PINK1 and Parkin, two Parkinson’s disease–associated proteins, mediate local mitophagy of dysfunctional mitochondria in neuronal axons. To reduce cytotoxicity and mimic physiological levels of mitochondrial damage, we selectively damaged a subset of mitochondria in hippocampal axons. Parkin was rapidly recruited to damaged mitochondria in axons followed by formation of LC3-positive autophagosomes and LAMP1-positive lysosomes. In PINK1−/− axons, damaged mitochondria did not accumulate Parkin and failed to be engulfed in autophagosomes. Similarly, initiation of mitophagy was blocked in Parkin−/− axons. Our findings demonstrate that the PINK1–Parkin-mediated pathway is required for local mitophagy in distal axons in response to focal damage. Local mitophagy likely provides rapid neuroprotection against oxidative stress without a requirement for retrograde transport to the soma.
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Axonal autophagy is dependent on specialized enzymatic apparatuses, including the PINK1-PRKN complex for localized mitophagy, KIF1A/UNC-104 for autophagosome formation at the synapse, and the HTT-HAP1 complex and MAPK8IP1/JIP1 for retrograde transport of autophagosomes.
“Axonal autophagy is dependent on specialized enzymatic apparatuses, including the PINK1-PRKN complex for localized mitophagy [24], KIF1A/UNC-104 for autophagosome formation at the synapse [22,25], and the HTT-HAP1 complex and MAPK8IP1/JIP1 for retrograde transport of autophagosomes [23,26].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [22]
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NIH Image to ImageJ: 25 years of image analysis
Schneider, C. A., Rasband, W. S., & Eliceiri, K. W. (2012) · Nature Methods · doi:10.1038/nmeth.2089 · Cited by 64,638 · see citing works
Autophagy: Renovation of Cells and Tissues
Mizushima, N., & Komatsu, M. (2011) · Cell · doi:10.1016/j.cell.2011.10.026 · Cited by 6,467 · see citing works
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 · see citing works
Chronic systemic pesticide exposure reproduces features of Parkinson's disease
Betarbet, R., Sherer, T., Mackenzie, G., Garcia-Osuna, M., Panov, A., & Greenamyre, J. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,797 · see citing works
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273 · see citing works
Wallace, D. C. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095751 · Cited by 3,185 · see citing works
PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944 · see citing works
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835 · see citing works
Autophagosome formation: core machinery and adaptations
Xie, Z., & Klionsky, D. J. (2007) · Nature Cell Biology · doi:10.1038/ncb1007-1102 · Cited by 2,165 · see citing works
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 · see citing works
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 · see citing works
Mitochondrial dynamics-fusion, fission, movement, and mitophagy-in neurodegenerative diseases
Chen, H., & Chan, D. C. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp326 · Cited by 1,455 · see citing works
PINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial Motility
Wang, X., Winter, D., Ashrafi, G., Schlehe, J. S., Wong, Y. L., Selkoe, D. J., Rice, S. E., Steen, J. A. J., LaVoie, M. J., & Schwarz, T. L. (2011) · Cell · doi:10.1016/j.cell.2011.10.018 · Cited by 1,161 · see citing works
Self-citationA microfluidic culture platform for CNS axonal injury, regeneration and transport
Taylor, A. M., Blurton-Jones, M. M., Rhee, S. W., Cribbs, D. H., Cotman, C. W., & Jeon, N. L. (2005) · Nature Methods · doi:10.1038/nmeth777 · Cited by 1,138 · see citing works
Dagda, R. K., Cherra, S. J., Kulich, S. M., Tandon, A., Park, D., & Chu, C. T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808515200 · Cited by 954 · see citing works
Parkin-deficient Mice Exhibit Nigrostriatal Deficits but Not Loss of Dopaminergic Neurons
Goldberg, M. S., Fleming, S. M., Palacino, J. J., Cepeda, C., Lam, H. A., Bhatnagar, A., Meloni, E. G., Wu, N., Ackerson, L. C., Klapstein, G. J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308947200 · Cited by 913 · see citing works
Keeney, P., Xie, J., Capaldi, R., & Bennett, J. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0984-06.2006 · Cited by 757 · see citing works
A Vesicular Transport Pathway Shuttles Cargo from Mitochondria to Lysosomes
Soubannier, V., McLelland, G., Zunino, R., Braschi, E., Rippstein, P. U., Fon, E. A., & McBride, H. M. (2012) · Current Biology · doi:10.1016/j.cub.2011.11.057 · Cited by 755 · see citing works
McLelland, G., Soubannier, V., Chen, C. X., McBride, H. M., & Fon, E. A. (2014) · The EMBO Journal · doi:10.1002/embj.201385902 · Cited by 743 · see citing works
Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment
Greene, A. W., Grenier, K., Aguileta, M. A., Muise, S., Farazifard, R., Haque, M. E., McBride, H. M., Park, D. S., & Fon, E. A. (2012) · The EMBO Reports · doi:10.1038/embor.2012.14 · Cited by 711 · cited 1× · see citing works
“PINK1 functions as a sensor for mitochondrial damage; its precursor is constitutively imported to the inner membrane of healthy mitochondria, where it is proteolytically cleaved (Greene et al., 2012) and eventually degraded by the protea some (Yamano and Youle, 2013).”
Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons
Maday, S., Wallace, K. E., & Holzbaur, E. L. F. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201106120 · Cited by 681 · cited 6× · see citing works
“S2, B and C) as previously observed (Maday et al., 2012).”
BackgroundResultInfluentialCraig, A. M., & Banker, G. A. (1994) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.17.030194.001411 · Cited by 678 · see citing works
Legros, F., Lombès, A., Frachon, P., & Rojo, M. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-06-0330 · Cited by 676 · see citing works
PINK1 is degraded through the N-end rule pathway
Yamano, K., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.24633 · Cited by 669 · see citing works
Glater, E. E., Megeath, L. J., Stowers, R. S., & Schwarz, T. L. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601067 · Cited by 667 · see citing works
Self-citationAxonal Transport of Mitochondria to Synapses Depends on Milton, a Novel Drosophila Protein
Stowers, R. S., Megeath, L. J., Górska‐Andrzejak, J., Meinertzhagen, I. A., & Schwarz, T. L. (2002) · Neuron · doi:10.1016/s0896-6273(02)01094-2 · Cited by 643 · see citing works
Self-citationA genetically encoded photosensitizer
Bulina, M. E., Chudakov, D. M., Britanova, O. V., Yanushevich, Y. G., Staroverov, D. B., Chepurnykh, T. V., Merzlyak, E. M., Shkrob, M., Lukyanov, S., & Lukyanov, K. A. (2005) · Nature Biotechnology · doi:10.1038/nbt1175 · Cited by 590 · see citing works
Axonal mitochondrial transport and potential are correlated
Miller, K. E., & Sheetz, M. P. (2004) · Journal of Cell Science · doi:10.1242/jcs.01130 · Cited by 512 · see citing works
Axon degeneration in Parkinson's disease
Burke, R. E., & O’Malley, K. L. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.01.011 · Cited by 494 · see citing works
Almeida, Á., Moncada, S., & Bolaños, J. P. (2003) · Nature Cell Biology · doi:10.1038/ncb1080 · Cited by 481 · see citing works
The PINK1-Parkin pathway promotes both mitophagy and selective respiratory chain turnover in vivo
Vincow, E. S., Merrihew, G., Thomas, R. E., Shulman, N. J., Beyer, R. P., MacCoss, M. J., & Pallanck, L. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221132110 · Cited by 478 · see citing works
Lee, S., Satō, Y., & Nixon, R. A. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6412-10.2011 · Cited by 471 · see citing works
Wang, Y., Nartiss, Y., Steipe, B., McQuibban, G. A., & Kim, P. K. (2012) · Autophagy · doi:10.4161/auto.21211 · Cited by 427 · see citing works
Almeida, A., Almeida, J., Bolaños, J. P., & Moncada, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261560998 · Cited by 423 · see citing works
Visualization of Retroviral Replication in Living Cells Reveals Budding into Multivesicular Bodies
Sherer, N. M., Lehmann, M. J., Soto, L. F. J., Ingmundson, A., Horner, S. M., Cicchetti, G., Allen, P. G., Pypaert, M., Cunningham, J. M., & Mothes, W. (2003) · Traffic · doi:10.1034/j.1600-0854.2003.00135.x · Cited by 411 · see citing works
Mitochondrial Trafficking to Synapses in Cultured Primary Cortical Neurons
Chang, D. T. W., Honick, A. S., & Reynolds, I. J. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1012-06.2006 · Cited by 391 · see citing works
Mitochondrial Parkin recruitment is impaired in neurons derived from mutant PINK1 iPS cells
Seibler, P., Graziotto, J., Jeong, H., Šimunović, F., Klein, C., & Krainc, D. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4441-10.2011 · Cited by 384 · see citing works
Soubannier, V., Rippstein, P. U., Kaufman, B. A., Shoubridge, E. A., & McBride, H. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052830 · Cited by 346 · see citing works
Cai, Q., Zakaria, H. M., Simone, A., & Sheng, Z. (2012) · Current Biology · doi:10.1016/j.cub.2012.02.005 · Cited by 332 · see citing works
Microfluidic Local Perfusion Chambers for the Visualization and Manipulation of Synapses
Taylor, A. M., Dieterich, D. C., Ito, H., Kim, S. A., & Schuman, E. M. (2010) · Neuron · doi:10.1016/j.neuron.2010.03.022 · Cited by 292 · see citing works
Weihofen, A., Craig, K. J. T., Ostaszewski, B. L., Cookson, M., & Selkoe, D. J. (2009) · Biochemistry · doi:10.1021/bi8019178 · Cited by 290 · see citing works
MPTP as a Mitochondrial Neurotoxic Model of Parkinson's Disease
Przedborski, S., Tieu, K., Perier, C., & Vila, M. (2004) · Journal of Bioenergetics and Biomembranes · doi:10.1023/b:jobb.0000041771.66775.d5 · Cited by 289 · see citing works
The mechanism of action of the respiratory inhibitor, antimycin
Slater, E. C. (1973) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(73)90002-5 · Cited by 280 · see citing works
A neo-substrate that amplifies catalytic activity of Parkinson's-disease-related kinase PINK1
Hertz, N. T., Berthet, A., Sos, M. L., Thorn, K. S., Burlingame, A. L., Nakamura, K., & Shokat, K. M. (2013) · Cell · doi:10.1016/j.cell.2013.07.030 · Cited by 275 · see citing works
Glucose Regulates Mitochondrial Motility via Milton Modification by O-GlcNAc Transferase
Pekkurnaz, G., Trinidad, J. C., Wang, X., Kong, D., & Schwarz, T. L. (2014) · Cell · doi:10.1016/j.cell.2014.06.007 · Cited by 271 · see citing works
Self-citationAxonal and dendritic endocytic pathways in cultured neurons.
Parton, R. G., Simons, K., & Dotti, C. G. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.119.1.123 · Cited by 269 · see citing works
Regulation of mitochondrial matrix volume
Kaasik, A., Safiulina, D., Zharkovsky, A., & Veksler, V. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00272.2006 · Cited by 259 · see citing works
Local Pruning of Dendrites and Spines by Caspase-3-Dependent and Proteasome-Limited Mechanisms
Ertürk, A., Wang, Y., & Sheng, M. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.3121-13.2014 · Cited by 231 · see citing works
Laar, V. S. V., Arnold, B. A., Cassady, S. J., Chu, C. T., Burton, E. A., & Berman, S. B. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq531 · Cited by 221 · see citing works
Rakovic, A., Shurkewitsch, K., Seibler, P., Grünewald, A., Zanon, A., Hagenah, J., Krainc, D., & Klein, C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.391680 · Cited by 218 · see citing works
A further update on the role of excitotoxicity in the pathogenesis of Parkinson’s disease
Ambrosi, G., Cerri, S., & Blandini, F. (2014) · Journal of Neural Transmission · doi:10.1007/s00702-013-1149-z · Cited by 195 · see citing works
Mitophagy Selectively Degrades Individual Damaged Mitochondria After Photoirradiation
Kim, I., & Lemasters, J. J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3768 · Cited by 193 · see citing works
The ubiquitin E3 ligase parkin regulates the proapoptotic function of Bax
Johnson, B. N., Berger, A. K., Cortese, G. P., & LaVoie, M. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113248109 · Cited by 189 · see citing works
Self-citationVerburg, J., & Hollenbeck, P. J. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2614-08.2008 · Cited by 150 · see citing works
Navarro, A., Boveris, A., Bández, M. J., Sánchez-del-Pino, M. J., Gómez, C., Muntané, G., & Ferrer, I. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.03.007 · Cited by 136 · see citing works
What causes the death of dopaminergic neurons in Parkinson’s disease?
Surmeier, D. J., Guzmán, J. N., Sánchez-Padilla, J., & Goldberg, J. A. (2010) · Progress in brain research · doi:10.1016/s0079-6123(10)83004-3 · Cited by 128 · see citing works
Parkin- and PINK1-Dependent Mitophagy in Neurons: Will the Real Pathway Please Stand Up?
Grenier, K., McLelland, G., & Fon, E. A. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00100 · Cited by 120 · see citing works
Ferree, A. W., Trudeau, K. M., Zik, E., Benador, I. Y., Twig, G., Gottlieb, R. A., & Shirihai, O. S. (2013) · Autophagy · doi:10.4161/auto.26503 · Cited by 119 · see citing works
In VivoImaging of Disease-Related Mitochondrial Dynamics in a Vertebrate Model System
Plucińska, G., Paquet, D., Hruscha, A., Godinho, L., Haass, C., Schmid, B., & Misgeld, T. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1327-12.2012 · Cited by 103 · see citing works
Parkin selectively alters the intrinsic threshold for mitochondrial cytochrome c release
Berger, A. K., Cortese, G. P., Amodeo, K. D., Weihofen, A., Letai, A. G., & LaVoie, M. J. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp384 · Cited by 83 · see citing works
Self-citationSpatiotemporally controlled initiation of Parkin-mediated mitophagy within single cells
Yang, J., & Yang, W. Y. (2011) · Autophagy · doi:10.4161/auto.7.10.16626 · Cited by 56 · see citing works
Bains, M., & Heidenreich, K. A. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)04007-x · Cited by 34 · see citing works
A Genetic Model to Dissect the Role of Tsc-mTORC1 in Neuronal Cultures
Nie, D. A., & Şahin, M. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-430-8_25 · Cited by 17 · see citing works
Recognizing the cooperative and independent mitochondrial functions of Parkin and PINK1
Johnson, B. N., Charan, R. A., & LaVoie, M. J. (2012) · Cell Cycle · doi:10.4161/cc.21261 · Cited by 16 · see citing works
Self-citation
Flagged first, then by citations
1 of the 65 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · see citing works
The Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease
Pickrell, A. M., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.007 · Cited by 2,310 · see citing works
Molecular mechanisms and physiological functions of mitophagy
Onishi, M., Yamano, K., Sato, M., Matsuda, N., & Okamoto, K. (2021) · The EMBO Journal · doi:10.15252/embj.2020104705 · Cited by 1,429 · see citing works
Selective neuronal vulnerability in Parkinson disease
Surmeier, D. J., Obeso, J. A., & Halliday, G. M. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.178 · Cited by 1,120 · see citing works
Compromised autophagy and neurodegenerative diseases
Menzies, F. M., Fleming, A., & Rubinsztein, D. C. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3961 · Cited by 851 · see citing works
Axonal transport: cargo-specific mechanisms of motility and regulation
Maday, S., Twelvetrees, A. E., Moughamian, A. J., & Holzbaur, E. L. F. (2014) · Neuron · doi:10.1016/j.neuron.2014.10.019 · Cited by 683 · see citing works
Mitochondria at the neuronal presynapse in health and disease
Devine, M. J., & Kittler, J. T. (2018) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.170 · Cited by 615 · see citing works
Redox regulation of the immune response
Morris, G., Gevezova, M., Sarafian, V. S., & Maes, M. H. J. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00902-0 · Cited by 600 · see citing works
Promoting the clearance of neurotoxic proteins in neurodegenerative disorders of ageing
Boland, B., Yu, W. H., Corti, O., Mollereau, B., Henriques, A., Bézard, E., Pastores, G., Rubinsztein, D. C., Nixon, R. A., Duchen, M. R., et al. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.109 · Cited by 552 · see citing works
Mitostasis in Neurons: Maintaining Mitochondria in an Extended Cellular Architecture
Misgeld, T., & Schwarz, T. L. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.055 · Cited by 546 · see citing works
Self-citationThe role of PINK1–Parkin in mitochondrial quality control
Narendra, D. P., & Youle, R. J. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01513-9 · Cited by 580 · see citing works
Mitochondrial dysfunction and mitophagy in Parkinson's: from familial to sporadic disease
Ryan, B. J., Hoek, S., Fon, E. A., & Wade-Martins, R. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.02.003 · Cited by 524 · see citing works
Park, J.-S., Davis, R. L., & Sue, C. M. (2018) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-018-0829-3 · Cited by 516 · see citing works
Ge, P., Dawson, V. L., & Dawson, T. M. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00367-7 · Cited by 514 · see citing works
Spatiotemporal Control of ULK1 Activation by NDP52 and TBK1 during Selective Autophagy
Vargas, J. N. S., Wang, C., Bunker, E. N., Hao, L., Maric, D., Schiavo, G., Randow, F., & Youle, R. J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.02.010 · Cited by 469 · see citing works
Hsieh, C.-H., Shaltouki, A., Gonzalez, A. E., da Cruz, A. B., Burbulla, L. F., Lawrence, E. S., Schüle, B., Krainc, D., Palmer, T. D., & Wang, X. (2016) · Cell stem cell · doi:10.1016/j.stem.2016.08.002 · Cited by 459 · see citing works
Defects in trafficking bridge Parkinson’s disease pathology and genetics
Abeliovich, A., & Gitler, A. D. (2016) · Nature · doi:10.1038/nature20414 · Cited by 462 · see citing works
A Molecular Approach to Mitophagy and Mitochondrial Dynamics.
Yoo, S., & Jung, Y. (2018) · PubMed Central · doi:10.14348/molcells.2018.2277 · Cited by 447 · see citing works
Yao, R.-Q., Ren, C., Xia, Z.-F., & Yao, Y.-M. (2021) · Autophagy · doi:10.1080/15548627.2020.1725377 · Cited by 441 · see citing works
Hamacher‐Brady, A., & Brady, N. R. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2087-8 · Cited by 396 · see citing works
Spatially Stable Mitochondrial Compartments Fuel Local Translation during Plasticity
Rangaraju, V., Lauterbach, M. A., & Schuman, E. M. (2019) · Cell · doi:10.1016/j.cell.2018.12.013 · Cited by 355 · see citing works
Schöndorf, D. C., Ivanyuk, D., Baden, P., Sanchez-Martinez, A., De Cicco, S., Yu, C., Giunta, I., Schwarz, L. K., Di Napoli, G., Panagiotakopoulou, V., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.05.009 · Cited by 337 · see citing works
Moore, A. S., & Holzbaur, E. L. F. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523810113 · Cited by 351 · see citing works
Basal mitophagy is widespread in Drosophila but minimally affected by loss of Pink1 or parkin
Lee, J. J., Sánchez-Martínez, Á., Martinez, A., Benincá, C., Mayor, U., Clague, M. J., & Whitworth, A. J. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201801044 · Cited by 343 · see citing works
Stavoe, A. K. H., & Holzbaur, E. L. F. (2019) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100818-125242 · Cited by 328 · see citing works
Synaptic, Mitochondrial, and Lysosomal Dysfunction in Parkinson’s Disease
Nguyen, M., Wong, Y. C., Ysselstein, D., Severino, A., & Krainc, D. (2019) · Trends in Neurosciences · doi:10.1016/j.tins.2018.11.001 · Cited by 323 · see citing works
Autophagy and Alzheimer’s Disease
Li, Q., Liu, Y., & Sun, M. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0386-8 · Cited by 331 · see citing works
Pickrell, A. M., Huang, C.-H., Kennedy, S. R., Ordureau, A., Sideris, D. P., Hoekstra, J. G., Harper, J. W., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2015.06.034 · Cited by 327 · see citing works
PINK1 and Parkin: emerging themes in mitochondrial homeostasis.
McWilliams, T. G., & Muqit, M. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.03.013 · Cited by 315 · see citing works
Compartment-Specific Regulation of Autophagy in Primary Neurons
Maday, S., & Holzbaur, E. L. F. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.4401-15.2016 · Cited by 309 · see citing works
PINK1 import regulation; a fine system to convey mitochondrial stress to the cytosol
Sekine, S., & Youle, R. J. (2018) · BMC Biology · doi:10.1186/s12915-017-0470-7 · Cited by 308 · see citing works
PINK1 signalling rescues amyloid pathology and mitochondrial dysfunction in Alzheimer’s disease
Du, F., Yu, Q., Yan, S., Hu, G., Lue, L., Walker, D., Wu, L., Yan, S. F., Tieu, K., & Yan, S. S. (2017) · Brain · doi:10.1093/brain/awx258 · Cited by 306 · see citing works
Role and Mechanisms of Mitophagy in Liver Diseases
Ma, X., McKeen, T., Zhang, J., & Ding, W. (2020) · Cells · doi:10.3390/cells9040837 · Cited by 279 · see citing works
Parkin-mediated mitophagy in mutant hAPP neurons and Alzheimer's disease patient brains
Ye, X., Sun, X., Starovoytov, V., & Cai, Q. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv056 · Cited by 274 · see citing works
Energy matters: presynaptic metabolism and the maintenance of synaptic transmission
Li, S., & Sheng, Z. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-021-00535-8 · Cited by 273 · see citing works
Seirafi, M., Kozlov, G., & Gehring, K. (2015) · The FEBS Journal · doi:10.1111/febs.13249 · Cited by 256 · see citing works
Mitophagy in Alzheimer’s disease: Molecular defects and therapeutic approaches
Mary, A., Eysert, F., Checler, F., & Chami, M. (2023) · Molecular Psychiatry · doi:10.1038/s41380-022-01631-6 · Cited by 244 · see citing works
Programming axonal mitochondrial maintenance and bioenergetics in neurodegeneration and regeneration
Cheng, X., Huang, N., & Sheng, Z. (2022) · Neuron · doi:10.1016/j.neuron.2022.03.015 · Cited by 253 · see citing works
Mitophagy and mitochondrial integrity in cardiac ischemia-reperfusion injury
Yang, M., Linn, B. S., Zhang, Y., & Ren, J. T. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.05.007 · Cited by 250 · see citing works
Deficiency of parkin and PINK1 impairs age-dependent mitophagy in Drosophila
Cornelissen, T., Vilain, S., Vints, K., Gounko, N., Verstreken, P., & Vandenberghe, W. (2018) · eLife · doi:10.7554/elife.35878 · Cited by 239 · see citing works
The ubiquitin signal and autophagy: an orchestrated dance leading to mitochondrial degradation
Yamano, K., Matsuda, N., & Tanaka, K. (2016) · EMBO Reports · doi:10.15252/embr.201541486 · Cited by 239 · see citing works
Mitophagy pathways in health and disease
Killackey, S. A., Philpott, D. J., & Girardin, S. E. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202004029 · Cited by 236 · see citing works
KIF1A/UNC-104 Transports ATG-9 to Regulate Neurodevelopment and Autophagy at Synapses
Stavoe, A. K. H., Kargbo-Hill, S. E., Hall, D. H., & Colón-Ramos, D. A. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.06.012 · Cited by 211 · see citing works
Regulation of mitochondrial transport in neurons
Lin, M.-Y., & Sheng, Z. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.01.004 · Cited by 223 · see citing works
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 215 · 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
Mechanisms of selective autophagy and mitophagy: Implications for neurodegenerative diseases
Chu, C. T. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.015 · Cited by 218 · see citing works
A Ubl/ubiquitin switch in the activation of Parkin
Sauvé, V., Lilov, A., Seirafi, M., Vranas, M., Rasool, S., Kozlov, G., Sprules, T. J., Wang, J., Trempe, J., & Gehring, K. (2015) · The EMBO Journal · doi:10.15252/embj.201592237 · Cited by 208 · see citing works
Ordureau, A., Paulo, J. A., Zhang, J., An, H., Swatek, K. N., Cannon, J. R., Wan, Q., Komander, D., & Harper, J. W. (2020) · Molecular Cell · doi:10.1016/j.molcel.2019.11.013 · Cited by 198 · see citing works
Mitochondrial dynamics and transport in Alzheimer's disease
Flannery, P. J., & Trushina, E. V. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.06.009 · Cited by 198 · see citing works
Autophagy and ALS: mechanistic insights and therapeutic implications
Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189 · see citing works
“Axonal autophagy is dependent on specialized enzymatic apparatuses, including the PINK1-PRKN complex for localized mitophagy [24], KIF1A/ UNC-104 for autophagosome formation at the synapse [22,25],”
BackgroundMitochondrial heterogeneity and homeostasis through the lens of a neuron
Pekkurnaz, G., & Wang, X. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00594-w · Cited by 195 · see citing works
Koentjoro, B., Park, J.-S., & Sue, C. M. (2017) · Scientific Reports · doi:10.1038/srep44373 · Cited by 191 · see citing works
Pink1 disables the anti-fission machinery to segregate damaged mitochondria for mitophagy
Pryde, K. R., Smith, H. L., Chau, K.-Y., & Schapira, A. H. V. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201509003 · Cited by 185 · see citing works
Lin, M.-Y., Cheng, X., Tammineni, P., Xie, Y., Zhou, B., Cai, Q., & Sheng, Z. (2017) · Neuron · doi:10.1016/j.neuron.2017.04.004 · Cited by 183 · see citing works
Emerging role of mitophagy in human diseases and physiology
Um, J., & Yun, J. (2017) · BMB Reports · doi:10.5483/bmbrep.2017.50.6.056 · Cited by 181 · see citing works
Mechanisms Orchestrating Mitochondrial Dynamics for Energy Homeostasis
Yu, S. B., & Pekkurnaz, G. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.07.027 · Cited by 182 · see citing works
BNIP3L/NIX-mediated mitophagy protects against glucocorticoid-induced synapse defects
Choi, G. E., Lee, H. J., Chae, C. W., Cho, J. H., Jung, Y. H., Kim, J. S., Kim, S. Y., Lim, J. R., & Han, H. J. (2021) · Nature Communications · doi:10.1038/s41467-020-20679-y · Cited by 182 · see citing works
Autophagy and mitophagy in ALS
Evans, C. S., & Holzbaur, E. L. F. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.005 · Cited by 178 · see citing works
Sorrentino, Z. A., Giasson, B. I., & Chakrabarty, P. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01977-2 · Cited by 181 · see citing works
PINK1/Parkin mitophagy and neurodegeneration—what do we really know in vivo?
Whitworth, A. J., & Pallanck, L. J. (2017) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2017.01.016 · Cited by 179 · 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 dysfunction and cell death in neurodegenerative diseases through nitroxidative stress
Akbar, M. D., Essa, M. M., Daradkeh, G., Abdelmegeed, M. A., Choi, Y., Mahmood, L., & Song, B. (2016) · Brain Research · doi:10.1016/j.brainres.2016.02.016 · Cited by 176 · see citing works
Kuijpers, M., Kochlamazashvili, G., Stumpf, A., Puchkov, D., Swaminathan, A., Lucht, M. T., Krause, E., Maritzen, T., Schmitz, D., & Haucke, V. (2021) · Neuron · doi:10.1016/j.neuron.2020.10.005 · Cited by 170 · see citing works
Lewis, T. L., Turi, G. F., Kwon, S., Losonczy, A., & Polleux, F. (2016) · Current Biology · doi:10.1016/j.cub.2016.07.064 · Cited by 167 · see citing works
The role of mitochondria in axon development and regeneration
Smith, G. M., & Gallo, G. (2017) · Developmental Neurobiology · doi:10.1002/dneu.22546 · Cited by 170 · see citing works
Notoginsenoside R1 Ameliorates Diabetic Retinopathy through PINK1-Dependent Activation of Mitophagy
Zhou, P., Xie, W., Meng, X., Zhai, Y., Dong, X., Zhang, X., Sun, G., & Sun, X. (2019) · Cells · doi:10.3390/cells8030213 · Cited by 169 · see citing works
Targeting mitophagy in neurodegenerative diseases
Antico, O., Thompson, P. W., Hertz, N. T., Muqit, M. M. K., & Parton, L. E. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-024-01105-0 · Cited by 178 · see citing works
Defects in ER–endosome contacts impact lysosome function in hereditary spastic paraplegia
Allison, R. J., Edgar, J. R., Pearson, G., Rizo, T., Newton, T. M., Günther, S., Berner, F., Hague, J., Connell, J. W., Winkler, J., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201609033 · Cited by 166 · see citing works
Mitochondrial degradation and energy metabolism
Melser, S., Lavie, J., & Bénard, G. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.05.010 · Cited by 163 · see citing works
Alpha-synuclein delays mitophagy and targeting Miro rescues neuron loss in Parkinson’s models
Shaltouki, A., Hsieh, C.-H., Kim, M. J., & Wang, X. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1873-4 · Cited by 161 · see citing works
Congenital disorders of autophagy: an emerging novel class of inborn errors of neuro-metabolism.
Ebrahimi‐Fakhari, D., Saffari, A., Wahlster, L., Lu, J., Byrne, S., Hoffmann, G., Jungbluth, H., & Şahin, M. (2016) · Brain : a journal of neurology · doi:10.1093/brain/awv371 · Cited by 150 · see citing works
Mitophagy in Cerebral Ischemia and Ischemia/Reperfusion Injury
Shen, L., Gan, Q., Yang, Y., Reis, C., Zhang, Z., Xu, S., Zhang, T., & Sun, C. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.687246 · Cited by 157 · see citing works
Neuronal mitochondria transport Pink1 mRNA via synaptojanin 2 to support local mitophagy
Harbauer, A. B., Hees, J. T., Wanderoy, S., Segura, I., Gibbs, W., Cheng, Y., Ordonez, M., Cai, Z., Cartoni, R., Ashrafi, G., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.01.035 · Cited by 156 · see citing works
Self-citationMul1 restrains Parkin-mediated mitophagy in mature neurons by maintaining ER-mitochondrial contacts
Puri, R., Cheng, X., Lin, M.-Y., Huang, N., & Sheng, Z. (2019) · Nature Communications · doi:10.1038/s41467-019-11636-5 · Cited by 155 · see citing works
Degradation of engulfed mitochondria is rate-limiting in Optineurin-mediated mitophagy in neurons
Evans, C. S., & Holzbaur, E. L. (2020) · eLife · doi:10.7554/elife.50260 · Cited by 137 · see citing works
“We hypothesize that either long-term exposure to low doses (>2 hr) or short periods of high concentration of AA (Ashrafi et al., 2014) may disrupt mitochondrial bioenergetics causing axonal mitochondria to undergo mitophagy locally to preserve the health of the neuron.”
BackgroundInfluentialMitochondrial dysfunction in cardiac aging
Tocchi, A., Quarles, E. K., Basisty, N., Gitari, L., & Rabinovitch, P. S. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.07.009 · Cited by 151 · see citing works
Farfel-Becker, T., Roney, J. C., Cheng, X.-T., Li, S., Cuddy, S. R., & Sheng, Z.-H. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.06.013 · Cited by 152 · see citing works
Impaired Mitochondrial Dynamics and Mitophagy in Neuronal Models of Tuberous Sclerosis Complex
Ebrahimi-Fakhari, D., Saffari, A., Wahlster, L., Di Nardo, A., Turner, D., Lewis, T. L., Conrad, C., Rothberg, J. M., Lipton, J. O., Kölker, S., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.054 · Cited by 146 · see citing works
Hou, X., Fiesel, F. C., Truban, D., Castanedes Casey, M., Lin, W.-L., Soto, A. I., Tacik, P., Rousseau, L. G., Diehl, N. N., Heckman, M. G., et al. (2018) · Autophagy · doi:10.1080/15548627.2018.1461294 · Cited by 147 · see citing works
Miro phosphorylation sites regulate Parkin recruitment and mitochondrial motility
Shlevkov, E., Kramer, T., Schapansky, J., LaVoie, M. J., & Schwarz, T. L. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612283113 · Cited by 145 · see citing works
Self-citationRegulation of mitochondrial dynamics in astrocytes: Mechanisms, consequences, and unknowns
Jackson, J. G., & Robinson, M. B. (2017) · Glia · doi:10.1002/glia.23252 · Cited by 144 · see citing works
Autophagy in neurodegeneration: New insights underpinning therapy for neurological diseases
Corti, O., Blomgren, K., Poletti, A., & Beart, P. M. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15002 · Cited by 141 · see citing works
Mechanisms and roles of mitochondrial localisation and dynamics in neuronal function
Seager, R., Lee, L. J., Henley, J. M., & Wilkinson, K. A. (2020) · Neuronal Signaling · doi:10.1042/ns20200008 · Cited by 141 · see citing works
Synapses: The Brain’s Energy-Demanding Sites
Faria‐Pereira, A., & Morais, V. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073627 · Cited by 145 · see citing works
Role of the endolysosomal system in Parkinson’s disease
Vidyadhara, D. J., Lee, J. E., & Chandra, S. S. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14820 · Cited by 131 · see citing works
Lionaki, E., Markaki, M., Palikaras, K., & Tavernarakis, N. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.04.010 · Cited by 134 · see citing works
Behl, T., Makkar, R., Sehgal, A., Singh, S., Sharma, N., Zengin, G., BUNGAU, S. G., Andronie-Cioară, F. L., Munteanu, M. A., Brisc, M. C., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147432 · Cited by 134 · see citing works
Parkinson's disease: convergence on synaptic homeostasis
Soukup, S., Vanhauwaert, R., & Verstreken, P. (2018) · The EMBO Journal · doi:10.15252/embj.201898960 · Cited by 129 · see citing works
Mitochondrial quality control by the Pink1/Parkin system
Rüb, C., Wilkening, A., & Voos, W. (2017) · Cell and Tissue Research · doi:10.1007/s00441-016-2485-8 · Cited by 132 · see citing works
Sadeghian, M., Mastrolia, V., Haddad, A. R., Mosley, A. J., Mullali, G., Schiza, D., Sajic, M., Hargreaves, I. P., Heales, S., Duchen, M. R., et al. (2016) · Scientific Reports · doi:10.1038/srep33249 · Cited by 129 · see citing works
Zhuang, X., Wang, S.-F., Tan, Y., Song, J., Zhu, Z., Wang, Z., Wu, M.-Y., Cai, C.-Z., Huang, Z., Tan, J., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2322-6 · Cited by 129 · see citing works
Targeting mitophagy in Parkinson's disease
Clark, E. H., de la Torre, A. V., Hoshikawa, T., & Briston, T. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.014294 · Cited by 128 · see citing works
Mechanisms of neuronal homeostasis: Autophagy in the axon
Maday, S. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.047 · Cited by 123 · see citing works
Disruption of axonal transport in neurodegeneration
Berth, S. H., & Lloyd, T. E. (2023) · Journal of Clinical Investigation · doi:10.1172/jci168554 · Cited by 126 · see citing works
Mitochondrial Morphology Differences and Mitophagy Deficit in Murine Glaucomatous Optic Nerve
Coughlin, L., Morrison, R. S., Horner, P. J., & Inman, D. M. (2015) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.14-16126 · Cited by 124 · see citing works
Laar, V. S. V., Roy, N., Liu, A., Rajprohat, S., Arnold, B. A., Dukes, A. A., Holbein, C. D., & Berman, S. B. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.11.015 · Cited by 121 · see citing works
Motor proteins at the mitochondria–cytoskeleton interface
Kruppa, A. J., & Buß, F. (2021) · Journal of Cell Science · doi:10.1242/jcs.226084 · Cited by 121 · see citing works
Mitochondrial Biology and Neurological Diseases
Arun, S., Liu, L., & Donmez, G. (2016) · Current Neuropharmacology · doi:10.2174/1570159x13666150703154541 · Cited by 113 · see citing works
Autophagosome dynamics in neurodegeneration at a glance
Wong, Y. C., & Holzbaur, E. L. F. (2015) · Journal of Cell Science · doi:10.1242/jcs.161216 · Cited by 116 · see citing works
- Authors
- Ashrafi, G., Schlehe, J. S., LaVoie, M. J., & Schwarz, T. L.
- Affiliations
- Boston Children's Hospital (US)
- Brigham and Women's Hospital (US)
- Corresponding author
- Schwarz, Thomas L.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2014-08-25
- Volume
- 206
- Issue
- 5
- Pages
- 655-670
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC4151150
- OpenAlex
- W1992264711
- Cited by
- 502
- References
- 65
- Citations by year
- 2026: 18 · 2025: 22 · 2024: 39 · 2023: 25 · 2022: 39 · 2021: 53 · 2020: 53 · 2019: 51 · 2018: 49 · 2017: 49 · 2016: 51 · 2015: 46 · 2014: 7
- FWCI
- 38.33
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- Funders
- National Institute of General Medical Sciences (GM069808, R01GM069808)
- National Institute of Neurological Disorders and Stroke (R21NS069949, R01NS065013, NS065013, NS069949)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD-01866, P30HD018655)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- mitophagy, PINK1, Parkin, axons, mitochondrial damage, Parkinson's disease, autophagosomes, lysosomes, oxidative stress, neuroprotection, hippocampal neurons, retrograde transport, mitochondrial quality control
- MeSH terms
- PTEN-Induced Putative Kinase, Animals, Antimycin A, Autophagy, Axons, Cells, Cultured, Female, Lysosomes, Mice, Inbred C57BL, Microtubule-Associated Proteins, Mitochondria, Phagosomes, Protein Kinases, Veratridine, Rats, Sprague-Dawley, Mice, Knockout, Rats, Long-Evans, Protein Transport, Ubiquitin-Protein Ligases, Mice, Rats, Membrane Potential, Mitochondrial, Mice, 129 Strain, Mitophagy
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