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TBK1 controls autophagosomal engulfment of polyubiquitinated mitochondria through p62/SQSTM1 phosphorylation
Abstract
Selective autophagy adaptor proteins, including p62/SQSTM1, play pivotal roles in the targeted degradation of ubiquitinated proteins or organelles through the autophagy-lysosome system. However, how autophagy adaptors promote the autophagosomal engulfment of selected substrates is poorly understood. Here, we show that p62 phosphorylation at S403 is required for the efficient autophagosomal engulfment of polyubiquitinated mitochondria during Parkin-dependent mitophagy. p62 is able to interact with Parkin-recruited mitochondria without S403 phosphorylation under mitophagy-inducing conditions, but those mitochondria are not enclosed by autophagosomes. Intriguingly, the S403 phosphorylation occurs only in the early period of mitochondrial depolarization. Optineurin and TANK-binding kinase 1 (TBK1) are transiently recruited to the polyubiquitinated mitochondria, and the activated TBK1 phosphorylates p62 at S403. TBK1 inhibitor, BX795, prevents the p62-mediated autophagosomal engulfment of Parkin-recruited mitochondria. Our results suggest that TBK1-mediated S403 phosphorylation regulates the efficient autophagosomal engulfment of ubiquitinated mitochondria as an immediate response to the mitochondrial depolarization.
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“Additionally, TBK1 amplifies the signaling cascade for mitophagy by phosphorylating OPTN and SQSTM1 (which enhances binding to ubiquitin and LC3) and promoting TBK1 autophosphorylation in a positive-feedback manner [58,59].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [59]
In the citing paper
“Through its phosphorylation of the autophagy receptors OPTN, SQSTM1, and CALCOCO2/NDP52 (calcium binding and coiled-coil domain 2) [58,59,194], TBK1 regulates several aspects of autophagy, including macroautophagy, xenophagy and mitophagy [59,90,148,194–196].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [59]
In the citing paper
“Mitochondrial protein ubiquitination promotes mitochondrial recruitment of autophagy regulators and receptors such as TBK1 and optineurin (Heo et al., 2015, Matsumoto et al., 2015, Richter et al., 2016).”
From A Cell-Based High-Throughput Screening Identified Two Compounds that Enhance PINK1-Parkin Signaling (2020) · cites this paper as Matsumoto et al., 2015
Citations
Cites
Autophagy: Renovation of Cells and Tissues
Mizushima, N., & Komatsu, M. (2011) · Cell · doi:10.1016/j.cell.2011.10.026 · Cited by 6,615
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455
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
Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273
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
Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969
Self-citationSelective autophagy mediated by autophagic adapter proteins
Johansen, T., & Lamark, T. (2011) · Autophagy · doi:10.4161/auto.7.3.14487 · Cited by 1,788
Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
Tanaka, A., Cleland, M. M., Xu, S., Narendra, D. P., Suen, D.-F., Karbowski, M., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007013 · Cited by 1,369
Phosphorylation of the Autophagy Receptor Optineurin Restricts Salmonella Growth
Wild, P., Farhan, H., McEwan, D. G., Wagner, S., Rogov, V. V., Brady, N. R., Richter, B., Korac, J., Waidmann, O., Choudhary, C., et al. (2011) · Science · doi:10.1126/science.1205405 · Cited by 1,298
Cited by
Sorted by citations
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
Hardiman, O. M., Al‐Chalabi, A., Chiò, A., Corr, E. M., Logroscino, G., Robberecht, W., Shaw, P. J., Simmons, Z., & van den Berg, L. H. (2017) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.71 · Cited by 2,237
Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance
Pickles, S., Vigié, P., & Youle, R. J. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.004 · Cited by 2,081
The mechanisms and roles of selective autophagy in mammals
Vargas, J. N. S., Hamasaki, M., Kawabata, T., Youle, R. J., & Yoshimori, T. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00542-2 · Cited by 1,088
Heo, J.-M., Ordureau, A., Paulo, J. A., Rinehart, J., & Harper, J. W. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.016 · Cited by 906
Mitophagy and Alzheimer’s Disease: Cellular and Molecular Mechanisms
Kerr, J. S., Adriaanse, B. A., Greig, N. H., Mattson, M. P., Cader, M. Z., Bohr, V. A., & Fang, E. F. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.01.002 · Cited by 870
Regulation of selective autophagy: the p62/SQSTM1 paradigm
Lamark, T., Svenning, S., & Johansen, T. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170035 · Cited by 753
Deciphering the Molecular Signals of PINK1/Parkin Mitophagy
Nguyen, T. N., Padman, B. S., & Lazarou, M. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.05.008 · Cited by 758
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
Autophagy balances inflammation in innate immunity
Deretic, V., & Levine, B. (2018) · Autophagy · doi:10.1080/15548627.2017.1402992 · Cited by 563
Autophagy: The spotlight for cellular stress responses
Ravanan, P., Florance, I., & Talwar, P. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.08.029 · Cited by 595
A Molecular Approach to Mitophagy and Mitochondrial Dynamics.
Yoo, S., & Jung, Y. (2018) · PubMed · doi:10.14348/molcells.2018.2277 · Cited by 457
STING directly activates autophagy to tune the innate immune response
Liu, D., Wu, H., Wang, C., Li, Y., Tian, H., Siraj, S., Sehgal, S. A., Wang, X., Wang, J., Shang, Y., et al. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0251-z · Cited by 439
Sellier, C., Campanari, M., Julie Corbier, C., Gaucherot, A., Kolb‐Cheynel, I., Oulad‐Abdelghani, M., Ruffenach, F., Page, A., Ciura, S., Kabashi, E., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593350 · Cited by 414
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
Moore, A. S., & Holzbaur, E. L. F. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523810113 · Cited by 362
FIP200 Claw Domain Binding to p62 Promotes Autophagosome Formation at Ubiquitin Condensates
Turco, E., Witt, M., Abert, C., Bock-Bierbaum, T., Su, M.-Y., Trapannone, R., Sztacho, M., Danieli, A., Shi, X., Zaffagnini, G., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.035 · Cited by 346
TBK1: a new player in ALS linking autophagy and neuroinflammation
Oakes, J. A., Davies, M. C., & Collins, M. O. (2017) · Molecular Brain · doi:10.1186/s13041-017-0287-x · Cited by 319
Mechanisms of mitophagy: PINK1, Parkin, USP30 and beyond
Bingol, B., & Sheng, M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.015 · Cited by 340
Kageyama, S., Gudmundsson, S. R., Sou, Y., Ichimura, Y., Tamura, N., Kazuno, S., Ueno, T., Miura, Y., Noshiro, D., Abe, M., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20185-1 · Cited by 301
Wurzer, B., Zaffagnini, G., Fracchiolla, D., Turco, E., Abert, C., Romanov, J., & Martens, S. (2015) · eLife · doi:10.7554/elife.08941 · Cited by 290
p62/ SQSTM 1: ‘Jack of all trades’ in health and cancer
Sánchez‐Martín, P., Saito, T., & Komatsu, M. (2018) · FEBS Journal · doi:10.1111/febs.14712 · Cited by 248
The Role of Mitophagy in Innate Immunity
Gkikas, I., Palikaras, K., & Tavernarakis, N. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01283 · Cited by 248
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 253
Expanding the ubiquitin code through post‐translational modification
Herhaus, L., & Đikić, I. (2015) · EMBO Reports · doi:10.15252/embr.201540891 · Cited by 240
Deng, Z., Lim, J., Wang, Q., Purtell, K., Wu, S., Palomo, G. M., Tan, H., Manfredi, G., Zhao, Y., Peng, J., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1644076 · Cited by 237
Evolving and Expanding the Roles of Mitophagy as a Homeostatic and Pathogenic Process
Gustafsson, Å. B., & Dorn, G. W. (2018) · Physiological Reviews · doi:10.1152/physrev.00005.2018 · Cited by 235
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
TRIM23 mediates virus-induced autophagy via activation of TBK1
Sparrer, K. M. J., Gableske, S., Zurenski, M. A., Parker, Z. M., Full, F., Baumgart, G. J., Kato, J., Pacheco–Rodriguez, G., Liang, C., Pornillos, O., et al. (2017) · Nature Microbiology · doi:10.1038/s41564-017-0017-2 · Cited by 221
Gao, F., Almeida, S., & Lopez‐Gonzalez, R. (2017) · The EMBO Journal · doi:10.15252/embj.201797568 · Cited by 229
Mechanisms and roles of mitophagy in neurodegenerative diseases
Wang, Y., Liu, N., & Lu, B. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13140 · Cited by 217
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
“autophosphorylation in a positive-feedback manner [58,59].”
BackgroundInfluentialRAB7A phosphorylation by TBK1 promotes mitophagy via the PINK-PARKIN pathway
Heo, J.-M., Ordureau, A., Swarup, S., Paulo, J. A., Shen, K., Sabatini, D. M., & Harper, J. W. (2018) · Science Advances · doi:10.1126/sciadv.aav0443 · Cited by 199
LRRC25 inhibits type I IFN signaling by targeting ISG15‐associated RIG‐I for autophagic degradation
Du, Y., Duan, T., Feng, Y., Liu, Q., Lin, M., Cui, J., & Wang, R. (2017) · The EMBO Journal · doi:10.15252/embj.201796781 · Cited by 173
Seabright, A. P., Fine, N. H. F., Barlow, J. P., Lord, S. O., Musa, I., Gray, A., Bryant, J. A., Banzhaf, M., Lavery, G. G., Hardie, D. G., et al. (2020) · The FASEB Journal · doi:10.1096/fj.201903051r · Cited by 176
Bacterial Pathogens versus Autophagy: Implications for Therapeutic Interventions
Kimmey, J. M., & Stallings, C. L. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.10.008 · Cited by 167
p62/ SQSTM1 and Selective Autophagy in Cardiometabolic Diseases
Jeong, S., Zhang, X., Rodríguez-Vélez, A., Evans, T. D., & Razani, B. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7649 · Cited by 169
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 187
Martínez-Silva, M. D. L., Imhoff-Manuel, R. D., Sharma, A., Heckman, C. J., Shneider, N. A., Roselli, F., Zytnicki, D., & Manuel, M. (2018) · eLife · doi:10.7554/elife.30955 · Cited by 153
The role of TBK1 in cancer pathogenesis and anticancer immunity
Runde, A. P., Mack, R. M., Breslin, P., & Zhang, J. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02352-y · Cited by 159
Major review: Molecular genetics of primary open-angle glaucoma
Liu, Y., & Allingham, R. R. (2017) · Experimental Eye Research · doi:10.1016/j.exer.2017.05.002 · Cited by 156
p62-mediated phase separation at the intersection of the ubiquitin-proteasome system and autophagy
Danieli, A., & Martens, S. (2018) · Journal of Cell Science · doi:10.1242/jcs.214304 · Cited by 144
Mitophagy in neurological disorders
Zhang, L., Dai, L., & Li, D. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02334-5 · Cited by 143
Vaites, L. P., Paulo, J. A., Huttlin, E. L., & Harper, J. W. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00392-17 · Cited by 120
Mechanisms of neuronal homeostasis: Autophagy in the axon
Maday, S. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.047 · Cited by 130
Orchestration of selective autophagy by cargo receptors
Adriaenssens, E., Ferrari, L., & Martens, S. (2022) · Current Biology · doi:10.1016/j.cub.2022.11.002 · Cited by 122
Haack, T. B., Ignatius, E., Calvo‐Garrido, J., Iuso, A., Isohanni, P., Maffezzini, C., Lönnqvist, T. R. I., Suomalainen, A., Gorza, M., Kremer, L. S., et al. (2016) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2016.06.026 · Cited by 125
Nguyen, T. D., Shaid, S., Vakhrusheva, O., Koschade, S. E., Klann, K., Thölken, M., Baker, F., Zhang, J., Oellerich, T., Sürün, D., et al. (2018) · Blood · doi:10.1182/blood-2018-02-833475 · Cited by 122
Dysfunction of Optineurin in Amyotrophic Lateral Sclerosis and Glaucoma
Toth, R. P., & Atkin, J. D. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01017 · Cited by 114
Diverse Functions of Autophagy in Liver Physiology and Liver Diseases
Ke, P. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20020300 · Cited by 117
Mitophagy: A novel perspective for insighting into cancer and cancer treatment
Song, C., Pan, S., Zhang, J., Li, N., & Geng, Q. (2022) · Cell Proliferation · doi:10.1111/cpr.13327 · Cited by 120
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Hennig, P., Fenini, G., Filippo, M. D., Karakaya, T., & Beer, H. (2021) · Biomedicines · doi:10.3390/biomedicines9070707 · Cited by 121
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Ohnstad, A. E., Delgado, J. M., North, B. J., Nasa, I., Kettenbach, A. N., Schultz, S. W., & Shoemaker, C. J. (2020) · The EMBO Journal · doi:10.15252/embj.2020104948 · Cited by 111
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Kim, S., Ahn, D., Syed, G. H., & Siddiqui, A. (2017) · Mitochondrion · doi:10.1016/j.mito.2017.11.007 · Cited by 106
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Kimura, T., Mandell, M. A., & Deretic, V. P. (2016) · Journal of Cell Science · doi:10.1242/jcs.163758 · Cited by 106
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Gerbino, V., Kaunga, E., Ye, J., Canzio, D., O’Keeffe, S., Rudnick, N. D., Guarnieri, P., Lutz, C. M., & Maniatis, T. (2020) · Neuron · doi:10.1016/j.neuron.2020.03.005 · Cited by 102
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Turco, E., Fracchiolla, D., & Martens, S. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.07.027 · Cited by 107
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Wang, L., Qi, H., Tang, Y., & Shen, H. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.08.002 · Cited by 102
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Webster, C. P., Smith, E. F., Shaw, P. J., & Vos, K. J. D. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00123 · Cited by 108
Glucose starvation induces LKB1-AMPK-mediated MMP-9 expression in cancer cells
Endo, H., Owada, S., Inagaki, Y., Shida, Y., & Tatemichi, M. (2018) · Scientific Reports · doi:10.1038/s41598-018-28074-w · Cited by 97
Mitchell, G., Cheng, M. I., Chen, C., Nguyen, B. N., Whiteley, A. T., Kianian, S., Cox, J. S., Green, D. R., McDonald, K. L., & Portnoy, D. A. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1716055115 · Cited by 98
Kinase regulation by liquid–liquid phase separation
López-Palacios, T. P., & Andersen, J. L. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.11.009 · Cited by 95
Markovinović, A., Cimbro, R., Ljutić, T., Križ, J., Rogelj, B., & Munitić, I. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.04.005 · Cited by 95
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Budini, M., Buratti, E., Morselli, E., & Criollo, A. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00170 · Cited by 101
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Fernández‐Albarral, J. A., Ramirez, A. I., de Hoz, R., Matamoros, J. A., Salobrar‐García, E., Elvira‐Hurtado, L., López‐Cuenca, I., Sánchez-Puebla, L., Salazar, J. J., & Ramirez, J. M. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1354569 · Cited by 105
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Ke, P. (2020) · Cells · doi:10.3390/cells9040831 · Cited by 91
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Yang, S., Imamura, Y., Jenkins, R. W., Cañadas, I., Kitajima, S., Aref, A. R., Brannon, A., Oki, E., Castoreno, A. B., Zhu, Z., et al. (2016) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-15-0235 · Cited by 92
Rab35 GTPase recruits NDP52 to autophagy targets
Minowa‐Nozawa, A., Nozawa, T., Okamoto‐Furuta, K., Kohda, H., & Nakagawa, I. (2017) · The EMBO Journal · doi:10.15252/embj.201796463 · Cited by 89
Moya, G. E., Rivera, P. D., & Dittenhafer‐Reed, K. E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22137030 · Cited by 90
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Hashimoto, K., Simmons, A., Kajino‐Sakamoto, R., Tsuji, Y., & Ninomiya‐Tsuji, J. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6663 · Cited by 86
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Jaishankar, D., Yakoub, A. M., Yadavalli, T., Agelidis, A. M., Thakkar, N., Hadigal, S. R., Ames, J. M., & Shukla, D. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aan5861 · Cited by 86
Weil, R., Laplantine, E., Curic, S., & Génin, P. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01243 · Cited by 83
Preserving Lysosomal Function in the Aging Brain: Insights from Neurodegeneration
Peng, W., Minakaki, G., Nguyen, M., & Krainc, D. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00742-3 · Cited by 79
Structure and function of p62/SQSTM1 in the emerging framework of phase separation
Berkamp, S., Mostafavi, S., & Sachse, C. (2020) · FEBS Journal · doi:10.1111/febs.15672 · Cited by 85
Wu, X., Yang, Z., Zou, J., Gao, H., Shao, Z., Li, C., & Lei, P. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02179-x · Cited by 88
Maurel, C., Dangoumau, A., Marouillat, S., Brulard, C., Chami, A. A., Hergesheimer, R. C., Corcia, P., Blasco, H., Andres, C. R., & Vourc’h, P. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0856-0 · Cited by 80
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Darios, F. D., & Stévanin, G. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.033 · Cited by 78
Exploring the genetics and non-cell autonomous mechanisms underlying ALS/FTLD
Chen, H., Kankel, M. W., Su, S. C., Han, S., & Ofengeim, D. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0060-4 · Cited by 74
Abnormal Mitochondrial Quality Control in Neurodegenerative Diseases
Yan, X., Wang, B., Hu, Y., Wang, S., & Zhang, X. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00138 · Cited by 74
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Chauvin, S. D., Stinson, W. A., Platt, D. J., Poddar, S., & Miner, J. J. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104866 · Cited by 77
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Durand, J. K., Zhang, Q. H., & Baldwin, A. S. (2018) · Cells · doi:10.3390/cells7090139 · Cited by 73
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Herhaus, L. (2021) · Matrix Biology · doi:10.1016/j.matbio.2021.01.004 · Cited by 71
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Ke, P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123940 · Cited by 78
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Komatsu, M. (2022) · IUBMB Life · doi:10.1002/iub.2689 · Cited by 69
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Duarte, J. N. (2021) · Journal of Ophthalmology · doi:10.1155/2021/4581909 · Cited by 74
C9ORF72 is a GDP/GTP exchange factor for Rab8 and Rab39 and regulates autophagy
Corbier, C., & Sellier, C. (2016) · Small GTPases · doi:10.1080/21541248.2016.1212688 · Cited by 73
Evidence that phosphorylated ubiquitin signaling is involved in the etiology of Parkinson’s disease
Shiba‐Fukushima, K., Ishikawa, K., Inoshita, T., Izawa, N., Takanashi, M., Sato, S., Onodera, O., Akamatsu, W., Okano, H., Imai, Y., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx201 · Cited by 64
Self-citationSato, M., Sato, K., Tomura, K., Kosako, H., & Sato, K. (2018) · Nature Cell Biology · doi:10.1038/s41556-017-0008-9 · Cited by 70
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Metadata
- Authors
- Matsumoto, G., Shimogori, T., Hattori, N., & Nukina, N.
- Affiliations
- RIKEN Center for Brain Science (JP)
- Juntendo University (JP)
- Corresponding author
- Matsumoto, Gen
- Nukina, Nobuyuki
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2015-05-13
- Volume
- 24
- Issue
- 15
- Pages
- 4429-4442
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2167192779
- Cited by
- 317
- References
- 45
- Citations by year
- 2026: 19 · 2025: 25 · 2024: 21 · 2023: 35 · 2022: 31 · 2021: 31 · 2020: 38 · 2019: 28 · 2018: 39 · 2017: 27 · 2016: 19 · 2015: 4
- FWCI
- 23.26
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Human Molecular Genetics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- TBK1, p62, mitophagy, Parkin, optineurin, mitochondrial depolarization, selective autophagy, BX795, autophagy-lysosome system
- MeSH terms
- Sequestosome-1 Protein, Animals, Autophagy, Cell Line, Humans, Mitochondria, Phosphorylation, Protein Serine-Threonine Kinases, Mice, Knockout, Polyubiquitin, Ubiquitin-Protein Ligases, Adaptor Proteins, Signal Transducing, Mice, Mitophagy
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