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Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells
Open accessAbstract
Recognition of injured mitochondria for degradation by macroautophagy is essential for cellular health, but the mechanisms remain poorly understood. Cardiolipin is an inner mitochondrial membrane phospholipid. We found that rotenone, staurosporine, 6-hydroxydopamine and other pro-mitophagy stimuli caused externalization of cardiolipin to the mitochondrial surface in primary cortical neurons and SH-SY5Y cells. RNAi knockdown of cardiolipin synthase or of phospholipid scramblase-3, which transports cardiolipin to the outer mitochondrial membrane, decreased the delivery of mitochondria to autophagosomes. Furthermore, we found that the autophagy protein microtubule-associated-protein-1 light chain 3 (LC3), which mediates both autophagosome formation and cargo recognition, contains cardiolipin-binding sites important for the engulfment of mitochondria by the autophagic system. Mutation of LC3 residues predicted as cardiolipin-interaction sites by computational modelling inhibited its participation in mitophagy. These data indicate that redistribution of cardiolipin serves as an 'eat-me' signal for the elimination of damaged mitochondria from neuronal cells.
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“changes in LC3-II amounts are tissue- and cell context-dependent.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). (2016) · cites this paper as [145]
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In the citing paper
“In the absence of lysosomal protease inhibitors, starvation results in a modest increase (HEK 293 cells) or even a decrease (HeLa cells) in the amount of LC3-II. The use of inhibitors reveals that this apparent decrease is due to lysosome-dependent degradation.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). (2016) · cites this paper as [145]
Experimental — accuracy not yet measuredIn the citing paper
“Cardiolipin — a phospholipid that is normally segregated to the inner mitochondrial membrane and is essential to the maintenance of mitochondrial architecture and function — when herniated outside a damaged mitochondrial membrane, stimulates mitophagy, a process that eliminates dysfunctional mitochondria and promotes the formation of new mitochondria (79).”
From Connecting aging biology and inflammation in the omics era (2022) · cites this paper as [79]
In the citing paper
“It should also be mentioned that the translocation of cardiolipin from the inner to outer mitochondrial membrane is another event that can trigger mitophagy [144].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [144]
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“LC3 proteins are involved in autophagosome formation, with participation of GABARAP subfamily members in later stages of autophagosome formation [201].”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [201]
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Cites
VMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952
Trott, O., & Olson, A. J. (2010) · Journal of Computational Chemistry · doi:10.1002/jcc.21334 · Cited by 38,412
Molecular dynamics with coupling to an external bath
Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F., DiNola, A., & Haak, J. R. (1984) · The Journal of Chemical Physics · doi:10.1063/1.448118 · Cited by 31,057
A smooth particle mesh Ewald method
Essmann, U., Perera, L., Berkowitz, M., Darden, T., Lee, H.-C., & Pedersen, L. (1995) · The Journal of Chemical Physics · doi:10.1063/1.470117 · Cited by 21,378
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
WebLogo: A Sequence Logo Generator: Figure 1Preprint
Crooks, G. E., Hon, G. C., Chandonia, J., & Brenner, S. E. (2004) · Genome Research · doi:10.1101/gr.849004 · Cited by 12,418
The MARTINI Force Field: Coarse Grained Model for Biomolecular Simulations
Marrink, . J., Risselada, H. J., Yefimov, S., Tieleman, D. P., & de Vries, A. H. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp071097f · Cited by 5,641
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
The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003
Boeckmann, B. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg095 · Cited by 3,911
Evans, D. J., & Holian, B. L. (1985) · The Journal of Chemical Physics · doi:10.1063/1.449071 · Cited by 3,644
Flagged first, then by citations
Cited by
Sorted by citations
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894
Mechanism and medical implications of mammalian autophagy
Dikic, I., & Elazar, Z. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0003-4 · Cited by 2,771
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
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 2,897
Self-citationAutophagy in infection, inflammation and immunity
Deretic, V., Saitoh, T., & Akira, S. (2013) · Nature Reviews Immunology · doi:10.1038/nri3532 · Cited by 1,919
Molecular definitions of autophagy and related processes
Galluzzi, L., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cecconi, F., Choi, A. M., Chu, C. T., Codogno, P., Colombo, M. I., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796697 · Cited by 1,646
Self-citationAutophagy in major human diseases
Klionsky, D. J., Petroni, G., Amaravadi, R. K., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cadwell, K., Cecconi, F., Choi, A. M. K., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021108863 · Cited by 1,585
Self-citationMechanisms of mitophagy in cellular homeostasis, physiology and pathology
Palikaras, K., Lionaki, E., & Tavernarakis, N. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0176-2 · Cited by 1,556
The far-reaching scope of neuroinflammation after traumatic brain injury
Simon, D. W., McGeachy, M. J., Bayır, H., Clark, R. S. B., Loane, D. J., & Kochanek, P. M. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.13 · Cited by 1,190
Self-citationCargo recognition and degradation by selective autophagy
Gatica, D., Lahiri, V., & Klionsky, D. J. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0037-z · Cited by 1,067
Mitochondrial dynamics and mitochondrial quality control
Ni, H.-M., Williams, J. A., & Ding, W.-X. (2015) · Redox Biology · doi:10.1016/j.redox.2014.11.006 · Cited by 931
The mitophagy pathway and its implications in human diseases
Wang, S., Long, H., Hou, L., Feng, B., Ma, Z., Wu, Y., Zeng, Y., Cai, J., Zhang, D., & Zhao, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01503-7 · Cited by 991
Compromised autophagy and neurodegenerative diseases
Menzies, F. M., Fleming, A., & Rubinsztein, D. C. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3961 · Cited by 851
Autophagy-Dependent Ferroptosis: Machinery and Regulation
Liu, J., Kuang, F., Kroemer, G., Klionsky, D. J., Kang, R., & Tang, D. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.02.005 · Cited by 819
Mitochondria ROS and mitophagy in acute kidney injury
Su, L., Zhang, J., Gomez, H., Kellum, J. A., & Peng, Z. (2022) · Autophagy · doi:10.1080/15548627.2022.2084862 · Cited by 822
Alpha-synuclein: Pathology, mitochondrial dysfunction and neuroinflammation in Parkinson’s disease
Rocha, E. M., Miranda, B. D., & Sanders, L. H. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.04.004 · Cited by 801
Selective Autophagy: ATG8 Family Proteins, LIR Motifs and Cargo Receptors
Johansen, T., & Lamark, T. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.07.016 · Cited by 736
Ubiquitin-Dependent And Independent Signals In Selective Autophagy
Khaminets, A., Behl, C., & Đikić, I. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.08.010 · Cited by 754
Cellular mitophagy: Mechanism, roles in diseases and small molecule pharmacological regulation
Lü, Y., Li, Z., Zhang, S., Zhang, T., Liu, Y., & Zhang, L. (2023) · Theranostics · doi:10.7150/thno.79876 · Cited by 738
To Be or Not to Be? How Selective Autophagy and Cell Death Govern Cell Fate
Green, D. R., & Levine, B. (2014) · Cell · doi:10.1016/j.cell.2014.02.049 · Cited by 698
Metabolic control of cell death
Green, D. R., Galluzzi, L., & Kroemer, G. (2014) · Science · doi:10.1126/science.1250256 · Cited by 678
Mitophagy in human health, ageing and disease
Picca, A., Faitg, J., Auwerx, J., Ferrucci, L., & D’Amico, D. (2023) · Nature Metabolism · doi:10.1038/s42255-023-00930-8 · Cited by 635
Mitochondria in health, disease, and aging
Harrington, J. S., Ryter, S. W., Plataki, M. E., Price, D. R., & Choi, A. M. K. (2023) · Physiological Reviews · doi:10.1152/physrev.00058.2021 · Cited by 641
Mitophagy, Mitochondrial Homeostasis, and Cell Fate
Ma, K., Chen, G., Li, W., Kepp, O., Zhu, Y., & Chen, Q. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00467 · Cited by 623
Cleaning house: selective autophagy of organelles
Anding, A. L., & Baehrecke, E. H. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.02.016 · Cited by 576
Miao, R., Jiang, C., Chang, W. Y.-H., Zhang, H., An, J., Ho, F. Y., Chen, P., Zhang, H., Junqueira, C., Amgalan, D., et al. (2023) · Immunity · doi:10.1016/j.immuni.2023.10.004 · Cited by 589
Richardson, J. R., Fitsanakis, V. A., Westerink, R. H. S., & Kanthasamy, A. G. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02033-9 · Cited by 551
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
Emerging views of mitophagy in immunity and autoimmune diseases
Xu, Y., Shen, J., & Ran, Z. (2019) · Autophagy · doi:10.1080/15548627.2019.1603547 · Cited by 533
Selective autophagy of intracellular organelles: Recent research advances
Li, W., He, P., Huang, Y., Li, Y.-F., Lu, J., Li, M., Kurihara, H., Luo, Z., Meng, T., Onishi, M., et al. (2020) · Theranostics · doi:10.7150/thno.49860 · Cited by 523
Paradies, G., Paradies, V., Ruggiero, F. M., & Petrosillo, G. (2019) · Cells · doi:10.3390/cells8070728 · Cited by 543
Amyloid Beta and Phosphorylated Tau-Induced Defective Autophagy and Mitophagy in Alzheimer’s Disease
Reddy, P. H., & Oliver, D. M. (2019) · Cells · doi:10.3390/cells8050488 · Cited by 496
“However, there is mitophagic dysfunction in AD [2,17].”
BackgroundMitochondrial Uncoupling: A Key Controller of Biological Processes in Physiology and Diseases
Demine, S., Renard, P., & Arnould, T. (2019) · Cells · doi:10.3390/cells8080795 · Cited by 476
“Another example is the parkinsonian neurotoxin 6-OHDA (6-hydroxydopamine), which also induces a mild mitochondrial uncoupling (10%) without triggering mitophagy in neurons and SH-SY5Y cells [113].”
BackgroundComplex interplay between autophagy and oxidative stress in the development of pulmonary disease
Ornatowski, W., Lü, Q., Yegambaram, M., Flores, A. G., Zemskov, E. A., Maltepe, E., Fineman, J. R., Wang, T., & Black, S. M. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101679 · Cited by 484
Mitophagy in degenerative joint diseases
Sun, K., Jing, X., Guo, J., Yao, X., & Guo, F. (2020) · Autophagy · doi:10.1080/15548627.2020.1822097 · Cited by 471
Essential role for autophagy in life span extension
Madeo, F., Zimmermann, A., Maiuri, M. C., & Kroemer, G. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73946 · Cited by 464
Mitochondrial autophagy: molecular mechanisms and implications for cardiovascular disease
Li, A., Gao, M. Q., Liu, B., Qin, Y. H., Chen, L., Liu, H., Wu, H., & Gong, G. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04906-6 · Cited by 478
Lou, G., Palikaras, K., Lautrup, S., Scheibye‐Knudsen, M., Tavernarakis, N., & Fang, E. F. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.07.002 · Cited by 455
Chronic inflammation and the hallmarks of aging
Baechle, J. J., Chen, N., Makhijani, P., Winer, S., Furman, D., & Winer, D. A. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101755 · Cited by 471
Excitotoxicity, calcium and mitochondria: a triad in synaptic neurodegeneration
Verma, M., Lizama, B. N., & Chu, C. T. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-021-00278-7 · Cited by 451
Self-citationQuality control of the mitochondrion
Ng, M. Y. W., Wai, T., & Simonsen, A. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.02.009 · Cited by 468
A Molecular Approach to Mitophagy and Mitochondrial Dynamics.
Yoo, S., & Jung, Y. (2018) · PubMed · doi:10.14348/molcells.2018.2277 · Cited by 457
Yao, R.-Q., Ren, C., Xia, Z.-F., & Yao, Y.-M. (2021) · Autophagy · doi:10.1080/15548627.2020.1725377 · Cited by 441
Mitochondria and cell death-associated inflammation
Vringer, E., & Tait, S. W. G. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01094-w · Cited by 461
Role of Cardiolipin in Mitochondrial Signaling Pathways
Dudek, J. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00090 · Cited by 444
Mechanisms of Selective Autophagy
Lamark, T., & Johansen, T. (2021) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-120219-035530 · Cited by 429
Receptor-mediated mitophagy in yeast and mammalian systems
Liu, L., Sakakibara, K., Chen, Q., & Okamoto, K. (2014) · Cell Research · doi:10.1038/cr.2014.75 · Cited by 421
PHB2 (prohibitin 2) promotes PINK1-PRKN/Parkin-dependent mitophagy by the PARL-PGAM5-PINK1 axis
Yan, C., Gong, L., Chen, L., Xu, M., Hamdan, H. A., Tang, M., Désaubry, L., & Song, Z. (2019) · Autophagy · doi:10.1080/15548627.2019.1628520 · Cited by 431
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
Mitochondria in innate immune signaling
Banoth, B., & Cassel, S. L. (2018) · Translational Research · doi:10.1016/j.trsl.2018.07.014 · Cited by 410
Autophagy in metabolic disease and ageing
Kitada, M., & Koya, D. (2021) · Nature Reviews Endocrinology · doi:10.1038/s41574-021-00551-9 · Cited by 421
Diverse Cellular Roles of Autophagy
Morishita, H., & Mizushima, N. (2019) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100818-125300 · Cited by 376
Hamacher‐Brady, A., & Brady, N. R. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2087-8 · Cited by 410
Mitochondria: diversity in the regulation of the NLRP3 inflammasome
Gurung, P., Lukens, J. R., & Kanneganti, T.-D. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2014.11.008 · Cited by 393
The crosstalk between ferroptosis and mitochondrial dynamic regulatory networks
Li, J., Jia, Y., Ding, Y.-X., Bai, J., Cao, F., & Li, F. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.83348 · Cited by 417
PINK1/Parkin-mediated mitophagy in neurodegenerative diseases
Li, J., Yang, D., Li, Z., Zhao, M., Wang, D., Sun, Z., Wen, P., Dai, Y., Gou, F., Ji, Y., et al. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101817 · Cited by 406
Nuclear DNA damage signalling to mitochondria in ageing
Fang, E. F., Scheibye-Knudsen, M., Chua, K. F., Mattson, M. P., Croteau, D. L., & Bohr, V. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.14 · Cited by 387
Autophagy: An Essential Degradation Program for Cellular Homeostasis and Life
Chun, Y., & Kim, J. (2018) · Cells · doi:10.3390/cells7120278 · Cited by 396
The emerging, multifaceted role of mitophagy in cancer and cancer therapeutics
Panigrahi, D. P., Praharaj, P. P., Bhol, C. S., Mahapatra, K. K., Patra, S., Behera, B. P., Mishra, S. R., & Bhutia, S. K. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.07.015 · Cited by 379
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
A fluorescence-based imaging method to measure in vitro and in vivo mitophagy using mt-Keima
Sun, N., Malide, D. A., Liu, J., Rovira, I. I., Combs, C. A., & Finkel, T. (2017) · Nature Protocols · doi:10.1038/nprot.2017.060 · Cited by 350
Mitochondrial Quality Control and Disease: Insights into Ischemia-Reperfusion Injury
Anzell, A. R., Maizy, R., Przyklenk, K., & Sanderson, T. H. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0503-9 · Cited by 359
Hexokinase-II Positively Regulates Glucose Starvation-Induced Autophagy through TORC1 Inhibition
Roberts, D. J., Tan‐Sah, V. P., Ding, E., Smith, J. M., & Miyamoto, S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.019 · Cited by 337
Mitochondrial dysfunction: roles in skeletal muscle atrophy
Chen, X., Ji, Y., Liu, R., Zhu, X., Wang, K., Yang, X., Liu, B., Gao, Z., Huang, Y. H., Shen, Y., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04369-z · Cited by 362
Determinants and Functions of Mitochondrial Behavior
Labbè, K., Murley, A., & Nunnari, J. M. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155756 · Cited by 324
Cloonan, S. M., & Choi, A. M. K. (2016) · Journal of Clinical Investigation · doi:10.1172/jci81113 · Cited by 322
Molecular Mechanisms of Mitochondrial Autophagy/Mitophagy in the Heart
Saito, T., & Sadoshima, J. (2015) · Circulation Research · doi:10.1161/circresaha.116.303790 · Cited by 329
The pharmacological regulation of cellular mitophagy
Georgakopoulos, N., Wells, G., & Campanella, M. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2287 · Cited by 330
Metabolism and function of mitochondrial cardiolipin
Ren, M., Phoon, C. K. L., & Schlame, M. (2014) · Progress in Lipid Research · doi:10.1016/j.plipres.2014.04.001 · Cited by 310
ROS-dependent S-palmitoylation activates cleaved and intact gasdermin D
Du, G., Healy, L. B., David, L., Walker, C., El‐Baba, T. J., Lutomski, C. A., Goh, B., Gu, B., Pi, X., Devant, P., et al. (2024) · Nature · doi:10.1038/s41586-024-07373-5 · Cited by 317
Mitochondrial dysfunction in neurodegenerative diseases and the potential countermeasure
Wang, Y., Xu, E., Musich, P. R., & Lin, F. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13116 · Cited by 298
Enkavi, G., Javanainen, M., Kulig, W., Róg, T., & Vattulainen, I. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00538 · Cited by 293
Autophagy and mitophagy in cancer metabolic remodelling
Ferro, F., Servais, S., Besson, P., Roger, S., Dumas, J., & Brisson, L. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.029 · Cited by 288
Role and Mechanisms of Mitophagy in Liver Diseases
Ma, X., McKeen, T., Zhang, J., & Ding, W. (2020) · Cells · doi:10.3390/cells9040837 · Cited by 288
Cardiolipin, Mitochondria, and Neurological Disease
Falabella, M., Vernon, H. J., Hanna, M. G., Claypool, S. M., & Pitceathly, R. D. S. (2021) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2021.01.006 · Cited by 282
Calcium signaling and mitochondrial destabilization in the triggering of the NLRP3 inflammasome
Horng, T. (2014) · Trends in Immunology · doi:10.1016/j.it.2014.02.007 · Cited by 284
ER-Phagy: Quality Control and Turnover of Endoplasmic Reticulum
Chino, H., & Mizushima, N. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.02.001 · Cited by 285
Lipid metabolism and lipophagy in cancer
Maan, M., Peters, J. M., Dutta, M., & Patterson, A. D. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.02.097 · Cited by 282
Mitochondrial quality control in health and in Parkinson’s disease
Eldeeb, M. A., Thomas, R. A., Ragheb, M. A., Fallahi, A., & Fon, E. A. (2022) · Physiological Reviews · doi:10.1152/physrev.00041.2021 · Cited by 281
Mitochondria as a therapeutic target for ischemic stroke
He, Z., Ning, N., Zhou, Q., Khoshnam, S. E., & Farzaneh, M. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.11.005 · Cited by 272
Mitochondrial degradation: Mitophagy and beyond
Uoselis, L., Nguyen, T. N., & Lazarou, M. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.08.021 · Cited by 270
Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging
Leduc-Gaudet, J.-P., Hussain, S. N. A., Barreiro, E., & Gouspillou, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158179 · Cited by 268
“It should also be mentioned that the translocation of cardiolipin from the inner to outer mitochondrial membrane is another event that can trigger mitophagy [144].”
BackgroundMitophagy in Alzheimer’s Disease and Other Age-Related Neurodegenerative Diseases
Cai, Q., & Jeong, Y. Y. (2020) · Cells · doi:10.3390/cells9010150 · Cited by 270
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
Brügger, B. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035324 · Cited by 265
Wei, H., Liu, L., & Chen, Q. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.03.013 · Cited by 266
Regulation of PRKN-independent mitophagy
Terešak, P., Lapão, A., Subic, N., Boya, P., Elazar, Z., & Simonsen, A. (2021) · Autophagy · doi:10.1080/15548627.2021.1888244 · Cited by 256
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 253
Mitophagy in tumorigenesis and metastasis
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Metadata
- Authors
- Chu, C. T., Ji, J., Dagda, R. K., Jiang, J. F., Tyurina, Y. Y., Kapralov, A. A., Tyurin, V. A., Yanamala, N., Shrivastava, I. H., Mohammadyani, D., Qiang Wang, K. Z., Zhu, J., Klein-Seetharaman, J., Balasubramanian, K., Amoscato, A. A., Borisenko, G., Huang, Z., Gusdon, A. M., Cheikhi, A., Steer, E. K., Wang, R., Baty, C., Watkins, S., Bahar, I., Bayır, H., & Kagan, V. E.
- Affiliations
- University of Pittsburgh (US)
- Corresponding author
- Chu, Charleen T.
- Tyurina, Yulia Y.
- Bayır, Hülya
- Kagan, Valerian E.
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2013-09-15
- Volume
- 15
- Issue
- 10
- Pages
- 1197-1205
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC3806088
- OpenAlex
- W2135592618
- Cited by
- 1,083
- References
- 66
- Citations by year
- 2026: 75 · 2025: 96 · 2024: 102 · 2023: 87 · 2022: 83 · 2021: 105 · 2020: 104 · 2019: 82 · 2018: 73 · 2017: 85 · 2016: 60 · 2015: 65 · 2014: 59 · 2013: 6
- FWCI
- 46.15
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Public Health Service (U19AIO68021)
- National Institute on Aging (AG026389, F32AG030821, R01AG026389)
- National Heart, Lung, and Blood Institute (HL-70755, R01HL070755, R01HL094488)
- National Institute of General Medical Sciences (P20GM103554, P41GM103712)
- National Institute of Allergy and Infectious Diseases (U19AI068021)
- National Institute of Neurological Disorders and Stroke (NS065789, NS076511, R01NS061817, R01NS065789, NS061817, R56NS065789, R37NS061817, R01NS076511)
- National Institute of Environmental Health Sciences (R21ES021068, ES 020693, R01ES020693)
- National Institute for Occupational Safety and Health (R01 OH008282, OH008282)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R21HD057587)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- cardiolipin, mitophagy, mitochondrial outer membrane, LC3, cardiolipin synthase, autophagy, neurons, mitochondrial damage, autophagosome formation, rotenone, staurosporine, 6-hydroxydopamine
- MeSH terms
- Amino Acid Sequence, Animals, Autophagy, Biological Transport, Cardiolipins, Cells, Cultured, HeLa Cells, Humans, Mitochondria, Models, Molecular, Molecular Sequence Data, Neurons, Rotenone, Uncoupling Agents, Signal Transduction, Oxidopamine, Rats, Sprague-Dawley, Protein Structure, Tertiary, Cell Line, Tumor, Mitochondrial Membranes, Rats, Gene Knockdown Techniques, Mitophagy
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