Receptor-mediated mitophagy in yeast and mammalian systems
Open accessAbstract
Mitophagy, or mitochondria autophagy, plays a critical role in selective removal of damaged or unwanted mitochondria. Several protein receptors, including Atg32 in yeast, NIX/BNIP3L, BNIP3 and FUNDC1 in mammalian systems, directly act in mitophagy. Atg32 interacts with Atg8 and Atg11 on the surface of mitochondria, promoting core Atg protein assembly for mitophagy. NIX/BNIP3L, BNIP3 and FUNDC1 also have a classic motif to directly bind LC3 (Atg8 homolog in mammals) for activation of mitophagy. Recent studies have shown that receptor-mediated mitophagy is regulated by reversible protein phosphorylation. Casein kinase 2 (CK2) phosphorylates Atg32 and activates mitophagy in yeast. In contrast, in mammalian cells Src kinase and CK2 phosphorylate FUNDC1 to prevent mitophagy. Notably, in response to hypoxia and FCCP treatment, the mitochondrial phosphatase PGAM5 dephosphorylates FUNDC1 to activate mitophagy. Here, we mainly focus on recent advances in our understanding of the molecular mechanisms underlying the activation of receptor-mediated mitophagy and the implications of this catabolic process in health and disease.
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
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Decreased mitophagy is associated with aging across multiple species.
“Decreased mitophagy will result in longer-lived and more damage-prone mitochondria, and decreased mitophagy is associated with aging across multiple species (Gelino and Hansen, 2012; Liu et al., 2014; Richard et al., 2013).”
From Programmed cell death in aging (2015) · cites this paper as Liu et al., 2014
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827 · 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
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 · see citing works
Mitochondrial diseases in man and mouse
Wallace, D. C. (1999) · Science · doi:10.1126/science.283.5407.1482 · Cited by 3,060 · 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
(2001) · PubMed · Cited by 2,381 · see citing works
Oxidative damage and mitochondrial decay in aging.
Shigenaga, M. K., Hagen, T. M., & Ames, B. N. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.10771 · Cited by 2,055 · see citing works
Mitochondria: Dynamic Organelles in Disease, Aging, and Development
Chan, D. C. (2006) · Cell · doi:10.1016/j.cell.2006.06.010 · Cited by 1,987 · see citing works
Endonuclease G is an apoptotic DNase when released from mitochondria
Li, L. Y., Luo, X., & Wang, X. (2001) · Nature · doi:10.1038/35083620 · Cited by 1,787 · see citing works
During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
Gomes, L. C., Benedetto, G. D., & Scorrano, L. (2011) · Nature Cell Biology · doi:10.1038/ncb2220 · Cited by 1,735 · see citing works
Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells
Liu, L., Feng, D., Chen, G., Chen, M., Zheng, Q., Song, P., Ma, Q., Zhu, C., Wang, R., Qi, W., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2422 · Cited by 1,689 · see citing works
Self-citationMitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008084 · Cited by 1,375 · see citing works
Lemasters, J. J. (2005) · Rejuvenation Research · doi:10.1089/rej.2005.8.3 · Cited by 1,342 · see citing works
Nix is a selective autophagy receptor for mitochondrial clearance
Novak, I., Kirkin, V., McEwan, D. G., Zhang, J., Wild, P., Rozenknop, A., Rogov, V., Löhr, F., Popovic, D., Occhipinti, A., et al. (2010) · The EMBO Reports · doi:10.1038/embor.2009.256 · Cited by 1,309 · see citing works
Essential role for Nix in autophagic maturation of erythroid cells
Sandoval, H., Thiagarajan, P., Dasgupta, S. K., Schumacher, A., Prchal, J. T., Chen, M., & Wang, J. (2008) · Nature · doi:10.1038/nature07006 · Cited by 1,185 · see citing works
Rambold, A. S., Kostelecky, B., Elia, N., & Lippincott‐Schwartz, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107402108 · Cited by 1,144 · see citing works
Discovery of Atg5/Atg7-independent alternative macroautophagy
Nishida, Y., Arakawa, S., Fujitani, K., Yamaguchi, H., Mizuta, T., Kanaseki, T., Komatsu, M., Otsu, K., Tsujimoto, Y., & Shimizu, S. (2009) · Nature · doi:10.1038/nature08455 · Cited by 1,103 · see citing works
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., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2837 · Cited by 1,083 · see citing works
Wang, Z., Jiang, H., Chen, S., Du, F., & Wang, X. (2012) · Cell · doi:10.1016/j.cell.2011.11.030 · Cited by 949 · see citing works
Gegg, M. E., Cooper, J. M., Chau, K.-Y., Rojo, M., Schapira, A. H. V., & Taanman, J.-W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq419 · Cited by 910 · see citing works
Mitochondria-Anchored Receptor Atg32 Mediates Degradation of Mitochondria via Selective Autophagy
Okamoto, K., Kondo‐Okamoto, N., & Ohsumi, Y. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.06.013 · Cited by 867 · see citing works
Self-citationStructural Basis for Sorting Mechanism of p62 in Selective Autophagy
Ichimura, Y., Kumanomidou, T., Sou, Y.-S., Mizushima, T., Ezaki, J., Ueno, T., Kominami, E., Yamane, T., Tanaka, K., & Komatsu, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802182200 · Cited by 803 · see citing works
Atg32 Is a Mitochondrial Protein that Confers Selectivity during Mitophagy
Kanki, T., Wang, K., Cao, Y., Baba, M., & Klionsky, D. J. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.06.014 · Cited by 798 · see citing works
The Interplay Between Mitochondrial Dynamics and Mitophagy
Twig, G., & Shirihai, O. S. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3779 · Cited by 778 · see citing works
Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism.
Ježek, P., & Hlavatá, L. (2005) · International Journal of Biochemistry and Cell Biology · doi:10.1016/j.biocel.2005.05.013 · Cited by 771 · see citing works
Hanna, R. A., Quinsay, M. N., Orogo, A. M., Giang, K., Rikka, S., & Gustafsson, Å. B. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.322933 · Cited by 762 · see citing works
Sowter, H., Ratcliffe, P. J., Watson, P. H., Greenberg, A. H., & Harris, A. L. (2001) · PubMed · Cited by 711 · see citing works
Matsumoto, G., Wada, K., Okuno, M., Kurosawa, M., & Nukina, N. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.039 · Cited by 692 · see citing works
PINK1- and Parkin-mediated mitophagy at a glance
Jin, S. M., & Youle, R. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.093849 · Cited by 631 · see citing works
Chen, G., Han, Z., Feng, D., Chen, Y., Chen, L., Wu, H., Huang, L., Zhou, C., Cai, X., Fu, C., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.034 · Cited by 600 · see citing works
Self-citationDing, W.-X., Ni, H., Li, M., Liao, Y., Chen, X., Stolz, D. B., Dorn, G. W., & Yin, X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.119537 · Cited by 586 · see citing works
Mitochondrial Control of Cellular Life, Stress, and Death
Galluzzi, L., Kepp, O., Trojel‐Hansen, C., & Kroemer, G. (2012) · Circulation Research · doi:10.1161/circresaha.112.268946 · Cited by 545 · see citing works
Loss of iron triggers PINK1/Parkin‐independent mitophagy
Allen, G. F. G., Toth, R. L., James, J. L., & Ganley, I. G. (2013) · EMBO Reports · doi:10.1038/embor.2013.168 · Cited by 540 · see citing works
Mitochondrial Disorders in the Nervous System
DiMauro, S., & Schon, E. A. (2008) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.30.051606.094302 · Cited by 536 · see citing works
Postfertilization Autophagy of Sperm Organelles Prevents Paternal Mitochondrial DNA Transmission
Rawi, S. A., Louvet‐Vallée, S., Djeddi, A., Sachse, M., Culetto, E., Hajjar, C., Boyd, L., Legouis, R., & Galy, V. (2011) · Science · doi:10.1126/science.1211878 · Cited by 505 · see citing works
Zhu, Y., Maßen, S., Terenzio, M., Lang, V., Chen-Lindner, S., Eils, R., Novak, I., Đikić, I., Hamacher‐Brady, A., & Brady, N. R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.399345 · Cited by 491 · see citing works
Degradation of Paternal Mitochondria by Fertilization-Triggered Autophagy in C. elegans Embryos
Sato, M., & Sato, K. (2011) · Science · doi:10.1126/science.1210333 · Cited by 469 · see citing works
Recent Advances in the Genetics of Parkinson's Disease
Martin, I., Dawson, V. L., & Dawson, T. M. (2011) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-082410-101440 · Cited by 438 · see citing works
Structural basis of target recognition by Atg8/LC3 during selective autophagy
Noda, N. N., Kumeta, H., Nakatogawa, H., Satoo, K., Adachi, W., Ishii, J., Fujioka, Y., Ohsumi, Y., & Inagaki, F. (2008) · Genes to Cells · doi:10.1111/j.1365-2443.2008.01238.x · Cited by 428 · 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
Uth1p Is Involved in the Autophagic Degradation of Mitochondria
Bhatia‐Kiššová, I., Deffieu, M. S., Manon, S., & Camougrand, N. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406960200 · Cited by 418 · see citing works
Satoo, K., Noda, N. N., Kumeta, H., Fujioka, Y., Mizushima, N., Ohsumi, Y., & Inagaki, F. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.80 · Cited by 381 · see citing works
Reactive oxygen species: Destroyers or messengers?
Bartosz, G. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.11.009 · Cited by 379 · see citing works
Mitophagy in Yeast Occurs through a Selective Mechanism
Kanki, T., & Klionsky, D. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802403200 · Cited by 335 · see citing works
The E1B 19K/Bcl-2–binding Protein Nip3 is a Dimeric Mitochondrial Protein that Activates Apoptosis
Chen, G., Ray, R., Dubik, D., Shi, L. F., Cizeau, J., Bleackley, R. C., Saxena, S. P., Gietz, R. D., & Greenberg, A. H. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.12.1975 · Cited by 332 · see citing works
Impairing the bioenergetic status and the biogenesis of mitochondria triggers mitophagy in yeast
Priault, M., Salin, B., Schaëffer, J., Vallette, F. M., di Rago, J.-P., & Martinou, J. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401697 · Cited by 292 · see citing works
Kurihara, Y., Kanki, T., Aoki, Y., Hirota, Y., Saigusa, T., Uchiumi, T., & Kang, D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.280156 · Cited by 279 · see citing works
Tal, R., Winter, G., Ecker, N., Klionsky, D. J., & Abeliovich, H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m605940200 · Cited by 268 · see citing works
A Genomic Screen for Yeast Mutants Defective in Selective Mitochondria Autophagy
Kanki, T., Wang, K., Baba, M., Bartholomew, C. R., Lynch-Day, M. A., Du, Z., Geng, J., Mao, K., Yang, Z., Yen, W.-L., et al. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-03-0225 · Cited by 266 · see citing works
Rheb Regulates Mitophagy Induced by Mitochondrial Energetic Status
Melser, S., Chatelain, É. H., Lavie, J., Mahfouf, W., José, C., Obre, É., Goorden, S. M. I., Priault, M., Elgersma, Y., Rezvani, H. R., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.014 · Cited by 259 · see citing works
Intracellular generation of reactive oxygen species by mitochondria
Nohl, H., Gille, L., & Staniek, K. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.12.002 · Cited by 251 · see citing works
Mao, K., Wang, K., Liu, X., & Klionsky, D. J. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.05.024 · Cited by 247 · see citing works
Regulation of mitochondrial protein import by cytosolic kinases.
Schmidt, O., Harbauer, A. B., Rao, S., Eyrich, B., Zahedi, R., Stojanovski, D., Schönfisch, B., Guiard, B., Sickmann, A., Pfanner, N., et al. (2011) · Cell · doi:10.1016/j.cell.2010.12.015 · Cited by 244 · see citing works
Phosphorylation of Serine 114 on Atg32 mediates mitophagy
Aoki, Y., Kanki, T., Hirota, Y., Kurihara, Y., Saigusa, T., Uchiumi, T., & Kang, D. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-02-0145 · Cited by 222 · see citing works
BNIP3 subfamily BH3-only proteins: mitochondrial stress sensors in normal and pathological functions
Chinnadurai, G., Vijayalingam, S., & Gibson, S. B. (2008) · Oncogene · doi:10.1038/onc.2009.49 · Cited by 219 · 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
Two MAPK-signaling pathways are required for mitophagy in <i>Saccharomyces cerevisiae</i>
Mao, K., Wang, K., Zhao, M., Xu, T., & Klionsky, D. J. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201102092 · Cited by 189 · see citing works
Mendl, N., Occhipinti, A., Müller, M. M., Wild, P. S., Đikić, I., & Reichert, A. S. (2011) · Journal of Cell Science · doi:10.1242/jcs.076406 · Cited by 161 · see citing works
Farré, J., Burkenroad, A., Burnett, S. F., & Subramani, S. E. (2013) · EMBO Reports · doi:10.1038/embor.2013.40 · Cited by 159 · see citing works
Campbell, C. L., & Thorsness, P. E. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.16.2455 · Cited by 156 · see citing works
Casein kinase 2 is essential for mitophagy
Kanki, T., Kurihara, Y., Jin, X., Goda, T., Ono, Y., Aihara, M., Hirota, Y., Saigusa, T., Aoki, Y., Uchiumi, T., et al. (2013) · EMBO Reports · doi:10.1038/embor.2013.114 · Cited by 152 · see citing works
Liver injury in α1-antitrypsin deficiency: an aggregated protein induces mitochondrial injury
Perlmutter, D. H. (2002) · Journal of Clinical Investigation · doi:10.1172/jci16787 · Cited by 150 · see citing works
Autophagy-related Protein 32 Acts as Autophagic Degron and Directly Initiates Mitophagy
Kondo‐Okamoto, N., Noda, N. N., Suzuki, S. W., Nakatogawa, H., Takahashi, I., Matsunami, M., Hashimoto, A., Inagaki, F., Ohsumi, Y., & Okamoto, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.299917 · Cited by 146 · see citing works
Self-citationCell death and autophagy: Cytokines, drugs, and nutritional factors
Bursch, W., Karwan, A., Mayer, M., Dornetshuber, J., Fröhwein, U., Schulte‐Hermann, R., Fazi, B., Sano, F. D., Piredda, L., Piacentini, M., et al. (2008) · Toxicology · doi:10.1016/j.tox.2008.07.048 · Cited by 140 · see citing works
Bit-by-bit autophagic removal of parkin-labelled mitochondria
Yang, J., & Yang, W. Y. (2013) · Nature Communications · doi:10.1038/ncomms3428 · Cited by 140 · see citing works
Liver injury in α1-antitrypsin deficiency: an aggregated protein induces mitochondrial injury
Perlmutter, D. H. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216787 · Cited by 133 · see citing works
Mitophagy in neurodegeneration and aging
Palikaras, K., & Tavernarakis, N. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2012.00297 · Cited by 122 · see citing works
Glutathione Participates in the Regulation of Mitophagy in Yeast
Deffieu, M. S., Bhatia‐Kiššová, I., Salin, B., Galinier, A., Manon, S., & Camougrand, N. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.005181 · Cited by 121 · see citing works
Byrne, A. M., Lemasters, J. J., & Nieminen, A. (1999) · Hepatology · doi:10.1002/hep.510290521 · Cited by 120 · see citing works
Mitochondrial biology, degenerative diseases and aging
Wallace, D. C., Brown, M. D., Melov, S., Graham, B. H., & Lott, M. T. (1998) · BioFactors · doi:10.1002/biof.5520070303 · Cited by 119 · see citing works
Organelle degradation during the lens and erythroid differentiation is independent of autophagy
Matsui, M., Yamamoto, A., Kuma, A., Ohsumi, Y., & Mizushima, N. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.11.044 · Cited by 110 · see citing works
Yamaguchi, M., Noda, N. N., Nakatogawa, H., Kumeta, H., Ohsumi, Y., & Inagaki, F. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.113670 · Cited by 110 · see citing works
Drosophila as a Model to Study Mitochondrial Dysfunction in Parkinson's DiseasePreprint
Guo, M. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009944 · Cited by 106 · see citing works
Molecular signaling toward mitophagy and its physiological significance
Feng, D., Liu, L., Zhu, Y., & Chen, Q. (2013) · Experimental Cell Research · doi:10.1016/j.yexcr.2013.03.034 · Cited by 97 · see citing works
Self-citationProteolytic processing of Atg32 by the mitochondrial i-AAA protease Yme1 regulates mitophagy
Wang, K., Jin, M., Liu, X., & Klionsky, D. J. (2013) · Autophagy · doi:10.4161/auto.26281 · Cited by 92 · see citing works
Aup1-mediated regulation of Rtg3 during mitophagy
Journo, D., Mor, A., & Abeliovich, H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.048140 · Cited by 90 · see citing works
Takeda, K., Yoshida, T., Kikuchi, S., Nagao, K., Kokubu, A., Pluskal, T., Villar‐Briones, A., Nakamura, T., & Yanagida, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911055107 · Cited by 89 · see citing works
Phosphatidylinositol 4-Kinases Are Required for Autophagic Membrane Trafficking
Wang, K., Yang, Z., Liu, X., Mao, K., Nair, U., & Klionsky, D. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.371591 · Cited by 76 · see citing works
Autophagy receptors in developmental clearance of mitochondria
Novak, I., & Đikić, I. (2011) · Autophagy · doi:10.4161/auto.7.3.14509 · Cited by 74 · see citing works
Richard, V. R., Leonov, A., Beach, A., Burstein, M. T., Koupaki, O., Gomez-Perez, A., Levy, S., Pluska, L., Mattie, S., Rafeh, R., et al. (2013) · Aging · doi:10.18632/aging.100547 · Cited by 68 · see citing works
Eiyama, A., Kondo‐Okamoto, N., & Okamoto, K. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.04.030 · Cited by 68 · see citing works
Self-citationThe Iron-Sulfur Clusters in Escherichia coli Succinate Dehydrogenase Direct Electron Flow
Cheng, V. W. T., Ma, E., Zhao, Z., Rothery, R. A., & Weiner, J. H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604900200 · Cited by 62 · see citing works
Welter, E., Montino, M., Reinhold, R., Schlotterhose, P., Krick, R., Dudek, J., Rehling, P., & Thumm, M. (2013) · FEBS Journal · doi:10.1111/febs.12468 · Cited by 48 · see citing works
In yeast, loss of Hog1 leads to osmosensitivity of autophagy
Prick, T., Thumm, M., Köhrer, K., Häussinger, D., & Dahl, S. V. (2006) · Biochemical Journal · doi:10.1042/bj20051243 · Cited by 46 · see citing works
Mitophagy, mitochondrial dynamics and the general stress response in yeast
Müller, M., & Reichert, A. S. (2011) · Biochemical Society Transactions · doi:10.1042/bst0391514 · Cited by 43 · see citing works
Teh, B. T., Blennow, E., Giraud, S., Sahlén, S., Hii, S.-I., Brookwell, R., Brauch, H. B., Nordenskjöld, M., Larsson, C., & Nicol, D. L. (1998) · Genes Chromosomes and Cancer · doi:10.1002/(sici)1098-2264(199803)21:3 · Cited by 25 · see citing works
Glutathione participates in the regulation of mitophagy in yeast
Kiššová, I. B., & Camougrand, N. M. (2009) · Autophagy · doi:10.4161/auto.9065 · Cited by 23 · see citing works
Mitophagy and Disease: New Avenues for Pharmacological Intervention
Taylor, R., & Goldman, S. J. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211796904768 · Cited by 20 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Cargo 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 · see citing works
PINK1 deficiency impairs mitochondrial homeostasis and promotes lung fibrosis
Bueno, M., Lai, Y.-C., Romero, Y., Brands, J., St. Croix, C. M., Kamga, C., Corey, C., Herazo-Maya, J. D., Sembrat, J., Lee, J. S., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci74942 · Cited by 627 · see citing works
Programmed cell death in aging
Tower, J. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.04.002 · Cited by 426 · see citing works
Tang, C., Han, H., Yan, M., Zhu, S., Liu, J., Liu, Z., He, L., Tan, J., Liu, Y., Liu, H., et al. (2018) · Autophagy · doi:10.1080/15548627.2017.1405880 · Cited by 309 · see citing works
Activation of BNIP3-mediated mitophagy protects against renal ischemia–reperfusion injury
Tang, C., Han, H., Liu, Z., Liu, Y., Yin, L., Cai, J., He, L., Liu, Y., Chen, G., Zhang, Z., et al. (2019) · Cell Death & Disease · doi:10.1038/s41419-019-1899-0 · Cited by 219 · 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
Mechanisms of Selective Autophagy in Normal Physiology and Cancer
Mancias, J. D., & Kimmelman, A. C. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.02.027 · Cited by 196 · see citing works
Organelle-Specific Initiation of Autophagy
Sica, V., Galluzzi, L., Bravo-San Pedro, J. M., Izzo, V., Maiuri, M. C., & Kroemer, G. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.021 · Cited by 205 · see citing works
Mitophagy Directs Muscle-Adipose Crosstalk to Alleviate Dietary Obesity
Fu, T., Xu, Z., Liu, L., Guo, Q., Wu, H., Liang, X., Zhou, D., Xiao, L., Liu, L., Liu, Y., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.127 · Cited by 145 · see citing works
Self-citationJu, J.-S., Jeon, S.-I., Park, J.-Y., Lee, J.-Y., Lee, S.-C., Cho, K.-J., & Jeong, J.-M. (2016) · The Journal of Physiological Sciences · doi:10.1007/s12576-016-0440-9 · Cited by 125 · see citing works
Physical Exercise: A Novel Tool to Protect Mitochondrial Health
Sorriento, D., Di Vaia, E., & Iaccarino, G. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.660068 · Cited by 118 · see citing works
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 · see citing works
The Role of Mitophagy in Regulating Cell Death
Li, S., Zhang, J., Liu, C., Wang, Q., Yan, J., Hui, L., Jia, Q., Shan, H., Tao, L., & Zhang, M. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6617256 · Cited by 76 · see citing works
Targeting the Autophagy/Lysosomal Degradation Pathway in Parkinsons Disease
Rivero-Ríos, P., Madero-Pérez, Fernández, B., & Hilfiker, S. (2016) · Current Neuropharmacology · doi:10.2174/1570159x13666151030103027 · Cited by 69 · see citing works
Molecular mechanisms of mitophagy and its roles in neurodegenerative diseases
Li, X., Huang, L., Lan, J., Feng, X., Li, P., Wu, L., & Peng, Y. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2020.105240 · Cited by 57 · see citing works
- Authors
- Liu, L., Sakakibara, K., Chen, Q., & Okamoto, K.
- Affiliations
- Chinese Academy of Sciences (CN)
- The University of Osaka (JP)
- Corresponding author
- Chen, Quan
- Okamoto, Koji
- Venue
- Cell Research
- Published
- 2014-06-06
- Volume
- 24
- Issue
- 7
- Pages
- 787-795
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- PMC
- PMC4085769
- OpenAlex
- W2049172731
- Cited by
- 421
- References
- 88
- Citations by year
- 2026: 25 · 2025: 34 · 2024: 42 · 2023: 49 · 2022: 51 · 2021: 58 · 2020: 30 · 2019: 31 · 2018: 25 · 2017: 19 · 2016: 27 · 2015: 28 · 2014: 2
- FWCI
- 3.38
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell Research (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (25291045, 26840067, 25650067)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- mitophagy, Atg32, BNIP3, FUNDC1, LC3, ATG8, Atg11, casein kinase 2, Src kinase, PGAM5, protein phosphorylation, hypoxia, FCCP, yeast, mammalian cells, mitochondrial quality control
- MeSH terms
- Autophagy-Related Proteins, Autophagy-Related Protein 8 Family, Animals, Humans, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Phosphorylation, Proto-Oncogene Proteins, Saccharomyces cerevisiae, Cell Hypoxia, Apoptosis, Receptors, Cytoplasmic and Nuclear, src-Family Kinases, Mitochondrial Proteins, Tumor Suppressor Proteins, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, Casein Kinase II, Mitochondrial Dynamics, Mitophagy
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