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LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Open accessAbstract
Little is known about the protein constituents of autophagosome membranes in mammalian cells. Here we demonstrate that the rat microtubule-associated protein 1 light chain 3 (LC3), a homologue of Apg8p essential for autophagy in yeast, is associated to the autophagosome membranes after processing. Two forms of LC3, called LC3-I and -II, were produced post-translationally in various cells. LC3-I is cytosolic, whereas LC3-II is membrane bound. The autophagic vacuole fraction prepared from starved rat liver was enriched with LC3-II. Immunoelectron microscopy on LC3 revealed specific labelling of autophagosome membranes in addition to the cytoplasmic labelling. LC3-II was present both inside and outside of autophagosomes. Mutational analyses suggest that LC3-I is formed by the removal of the C-terminal 22 amino acids from newly synthesized LC3, followed by the conversion of a fraction of LC3-I into LC3-II. The amount of LC3-II is correlated with the extent of autophagosome formation. LC3-II is the first mammalian protein identified that specifically associates with autophagosome membranes.
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“As LC3II is a lipidated form of LC3 (Kabeya et al., 2000), these results indicated an increase in autophagosome formation.”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Kabeya et al., 2000
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“The cytosolic form of LC3 (designated LC3-I) is conjugated to phosphatidylethanolamine (PE) and in this form (designated LC3-II) it is recruited to the growing autophagosome membrane [26].”
From LC3-Associated Phagocytosis (LAP): Connections with Host Autophagy (2012) · cites this paper as [26]
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“Another alternative to mRFP or mCherry is to use the Venus variant of YFP, which is brighter than mRFP and less sensitive to pH than GFP.186”
From Guidelines for the use and interpretation of assays for monitoring autophagy (2012) · cites this paper as [186]
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Citations
Cites
Smith, D. B., & Johnson, K. S. (1988) · Gene · doi:10.1016/0378-1119(88)90005-4 · Cited by 5,844
Induction of autophagy and inhibition of tumorigenesis by beclin 1
Liang, X. H., Jackson, S., Seaman, M., Brown, K., Kempkes, B., Hibshoosh, H., & Levine, B. (1999) · Nature · doi:10.1038/45257 · Cited by 3,347
Isolation and characterization of autophagy‐defective mutants of Saccharomyces cerevisiae
Tsukada, M., & Ohsumi, Y. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80398-e · Cited by 1,837
Self-citationA protein conjugation system essential for autophagy
Mizushima, N., Noda, T., Yoshimori, T., Tanaka, Y., Ishii, T., George, M. D., Klionsky, D. J., Ohsumi, M., & Ohsumi, Y. (1998) · Nature · doi:10.1038/26506 · Cited by 1,758
Self-citationYamamoto, A., Tagawa, Y., Yoshimori, T., Moriyama, Y., Masaki, R., & Tashiro, Y. (1998) · Cell Structure and Function · doi:10.1247/csf.23.33 · Cited by 1,312
Self-citationKirisako, T., Ichimura, Y., Okada, H., Kabeya, Y., Mizushima, N., Yoshimori, T., Ohsumi, M., Takao, T., Noda, T., & Ohsumi, Y. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.2.263 · Cited by 1,024
Self-citationFormation Process of Autophagosome Is Traced with Apg8/Aut7p in Yeast
Kirisako, T., Baba, M., Ishihara, N., Miyazawa, K., Ohsumi, M., Yoshimori, T., Noda, T., & Ohsumi, Y. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.2.435 · Cited by 881
Self-citationGABAA-receptor-associated protein links GABAA receptors and the cytoskeleton
Wang, H.-B., Bedford, F., Brandon, N., Moss, S., & Olsen, R. (1999) · Nature · doi:10.1038/16264 · Cited by 754
Autophagy and related mechanisms of lysosome-mediated protein degradation
Dunn, W. A. (1994) · Trends in Cell Biology · doi:10.1016/0962-8924(94)90069-8 · Cited by 534
A New Protein Conjugation System in Human
Mizushima, N., Sugita, H., Yoshimori, T., & Ohsumi, Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.33889 · Cited by 521
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Items 1,001–1,091 of 1,091
Timosaponin A-III Induces Autophagy Preceding Mitochondria-Mediated Apoptosis in HeLa Cancer Cells
Sy, L., Yan, S., Lok, C., Man, R. Y. K., & Che, C. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1983 · Cited by 142
Regulation of Autophagy and Its Associated Cell Death by “Sphingolipid Rheostat”
Taniguchi, M., Kitatani, K., Kondo, T., Hashimoto-Nishimura, M., Asano, S., Hayashi, A., Mitsutake, S., Igarashi, Y., Umehara, H., Takeya, H., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.416552 · Cited by 140
Beclin 1 and LC3 autophagic gene expression in cutaneous melanocytic lesions
Miracco, C., Cevenini, G., Franchi, A., Luzi, P., Cosci, E., Mourmouras, V., Monciatti, I., Mannucci, S., Biagioli, M., Toscano, M., et al. (2010) · Human Pathology · doi:10.1016/j.humpath.2009.09.004 · Cited by 139
Oligemic Hypoperfusion Differentially Affects Tau and Amyloid-β
Koike, M. A., Green, K. N., Blurton-Jones, M., & LaFerla, F. M. (2010) · The American Journal of Pathology · doi:10.2353/ajpath.2010.090750 · Cited by 130
Chen, X., Wang, K., Xing, Y., Tu, J., Yang, X., Zhao, Q., Li, K., & Chen, Z. (2014) · Protein & Cell · doi:10.1007/s13238-014-0104-6 · Cited by 130
Kanno, H., Ozawa, H., Sekiguchi, A., Yamaya, S., & Itoi, E. (2011) · Spine · doi:10.1097/brs.0b013e3182028c3a · Cited by 131
Casein kinase 1α: biological mechanisms and theranostic potential
Jiang, S., Zhang, M., Sun, J., & Yang, X. (2018) · Cell Communication and Signaling · doi:10.1186/s12964-018-0236-z · Cited by 130
Zulauf, K. E., Sullivan, J. T., & Braunstein, M. (2018) · PLOS Pathogens · doi:10.1371/journal.ppat.1007011 · Cited by 120
SKD1 AAA ATPase-Dependent Endosomal Transport is Involved in Autolysosome Formation.
Nara, A., Mizushima, N., Yamamoto, A., Kabeya, Y., Ohsumi, Y., & Yoshimori, T. (2002) · Cell Structure and Function · doi:10.1247/csf.27.29 · Cited by 144
Self-citationSteele, S., Brunton, J., Ziehr, B., Taft-Benz, S., Moorman, N., & Kawula, T. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003562 · Cited by 123
Zhang, X., Garbett, K., Veeraraghavalu, K., Wilburn, B., Gilmore, R., Mirnics, K., & Sisodia, S. S. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0556-12.2012 · Cited by 122
Senescent Keratinocytes Die by Autophagic Programmed Cell Death
Gosselin, K., Deruy, E., Martien, S., Vercamer, C., Bouali, F., Dujardin, T., Slomianny, C., Houel-Renault, L., Chelli, F., De Launoit, Y., et al. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.080332 · Cited by 119
de la Cruz-Morcillo, M. A., Valero, M. L. L., Callejas-Valera, J. L., Arias-González, L., Melgar-Rojas, P., Galán-Moya, E. M., García-Gil, E., García-Cano, J., & Sánchez-Prieto, R. (2012) · Oncogene · doi:10.1038/onc.2011.321 · Cited by 117
RetractedLC3-Associated Phagocytosis (LAP): Connections with Host Autophagy
Lai, S.-C., & Devenish, R. J. (2012) · Cells · doi:10.3390/cells1030396 · Cited by 116
“The cytosolic form of LC3 (designated LC3-I) is conjugated to phosphatidylethanolamine (PE) and in this form (designated LC3-II) it is recruited to the growing autophagosome membrane [26].”
BackgroundA conserved mechanism of TOR-dependent RCK-mediated mRNA degradation regulates autophagy
Hu, G., McQuiston, T., Bernard, A., Park, Y.-D., Qiu, J., Vural, A., Zhang, N., Waterman, S. R., Blewett, N. H., Myers, T. G., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3189 · Cited by 116
Chakrabarti, L., Eng, J., Ivanov, N., Garden, G. A., & La Spada, A. R. (2009) · Molecular Brain · doi:10.1186/1756-6606-2-24 · Cited by 112
Shteingauz, A., Porat, Y., Voloshin, T., Schneiderman, R. S., Munster, M., Zeevi, E., Kaynan, N., Gotlib, K., Giladi, M., Kirson, E. D., et al. (2018) · Cell Death & Disease · doi:10.1038/s41419-018-1085-9 · Cited by 107
Yamada, E., Bastie, C. C., Koga, H., Wang, Y., Cuervo, A. M., & Pessin, J. E. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.03.014 · Cited by 103
Podocytes maintain high basal levels of autophagy independent of mtor signaling
Bork, T., Liang, W., Yamahara, K., Lee, P., Tian, Z., Liu, S., Schell, C., Thedieck, K., Hartleben, B., Patel, K., et al. (2020) · Autophagy · doi:10.1080/15548627.2019.1705007 · Cited by 100
Mieulet, V., Roceri, M., Espeillac, C., Sotiropoulos, A., Ohanna, M., Oorschot, V., Klumperman, J., Sandri, M., & Pende, M. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00499.2006 · Cited by 99
Dysregulated autophagy contributes to caspase-dependent neuronal apoptosis
Chung, Y., Lee, J., Jung, S., Lee, Y., Cho, J. W., & Oh, Y. J. (2018) · Cell Death & Disease · doi:10.1038/s41419-018-1229-y · Cited by 99
Fox, J. H., Connor, T., Chopra, V., Dorsey, K., Kama, J. A., Bleckmann, D., Betschart, C., Hoyer, D., Frentzel, S., DiFiglia, M., et al. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-26 · Cited by 94
“Both normalized LC3BII levels and the LC3BI: LC3BII ratio (conversion) have been used as measures of macroautophagy activation [22,23].”
BackgroundMethodMolitoris, J. K., McColl, K. S., Swerdlow, S., Matsuyama, M., Lam, M., Finkel, T. H., Matsuyama, S., & Distelhorst, C. W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.245423 · Cited by 96
Orosco, L. A., Ross, A. P., Cates, S. L., Scott, S. E., Wu, D., Sohn, J., Pleasure, D., Pleasure, S. J., Adamopoulos, I. E., & Zarbalis, K. S. (2014) · Nature Communications · doi:10.1038/ncomms5692 · Cited by 90
Role of Atg5-dependent cell death in the embryonic development of Bax/Bak double-knockout mice
Arakawa, S., Tsujioka, M., Yoshida, T., Tajima-Sakurai, H., Nishida, Y., Matsuoka, Y., Yoshino, I., Tsujimoto, Y., & Shimizu, S. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.84 · Cited by 94
Gao, W., Kang, J. H., Liao, Y., Ding, W.-X., Gambotto, A. A., Watkins, S. C., Liu, Y.-J., Stolz, D. B., & Yin, X.-M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.054197 · Cited by 94
Crosstalk between apoptosis and autophagy signaling pathways
(2020) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2020.01.003 · Cited by 92
Roscic, A., Baldo, B., Crochemore, C., Marcellin, D., & Paganetti, P. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07435.x · Cited by 92
Microgravity control of autophagy modulates osteoclastogenesis
Sambandam, Y., Townsend, M. T., Pierce, J. J., Lipman, C. M., Haque, A., Bateman, T. A., & Reddy, S. V. (2014) · Bone · doi:10.1016/j.bone.2014.01.004 · Cited by 93
Chen, H.-C., Fong, T.-H., Lee, A.-W., & Chiu, W.-T. (2012) · Spine · doi:10.1097/brs.0b013e318221e859 · Cited by 90
Jänen, S. B., Chaachouay, H., & Richter‐Landsberg, C. (2010) · Glia · doi:10.1002/glia.21047 · Cited by 87
Mitochondrial dynamics in cancer-induced cachexia
van der Ende, M., Grefte, S., Plas, R., Meijerink, J., Witkamp, R. F., Keijer, J., & van Norren, K. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.07.008 · Cited by 87
17-AAG Induces Cytoplasmic α-Synuclein Aggregate Clearance by Induction of Autophagy
Riedel, M., Goldbaum, O., Schwarz, L., Schmitt, S., & Richter-Landsberg, C. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008753 · Cited by 87
“The latter is a membrane-bound 16 kDa isoform which associates with the autophagosomal membranes and its amount as compared to tubulin or actin correlates with the number of autophagosomes [37,38].”
BackgroundMaki, T., Yamamoto, D., Nakanishi, S., Iida, K., Iguchi, G., Takahashi, Y., Kaji, H., Chihara, K., & Okimura, Y. (2012) · Nutrition Research · doi:10.1016/j.nutres.2012.07.005 · Cited by 85
Cann, G. M., Guignabert, C., Ying, L., Deshpande, N., Bekker, J. M., Wang, L., Zhou, B., & Rabinovitch, M. (2008) · Developmental Dynamics · doi:10.1002/dvdy.21392 · Cited by 84
Autophagy in Pulmonary Diseases
Nakahira, K., Pabon Porras, M. A., & Choi, A. M. K. (2016) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201512-2468so · Cited by 78
Li, W., Zou, W., Yang, Y., Chai, Y., Chen, B., Cheng, S., Tian, D., Wang, X., Vale, R. D., & Ou, G. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201111053 · Cited by 84
Impaired Mitophagy Plays a Role in Denervation of Neuromuscular Junctions in ALS Mice
Rogers, R. S., Tungtur, S., Tanaka, T., Nadeau, L. L., Badawi, Y., Wang, H., Ni, H.-M., Ding, W.-X., & Nishimune, H. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00473 · Cited by 83
“LC3 proteins accumulated as large puncta in NMJ presynaptic terminals in diaphragms of SOD1G93A mice (Figure 2A lower panels).”
BackgroundMethodInfluentialKanamori, H., Naruse, G., Yoshida, A., Minatoguchi, S., Watanabe, T., Kawaguchi, T., Yamada, Y., Mikami, A., Kawasaki, M., Takemura, G., et al. (2019) · Circulation: Heart Failure · doi:10.1161/circheartfailure.118.005418 · Cited by 84
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
Autophagy in traumatic brain injury: a new target for therapeutic intervention
Zhang, L., & Wang, H. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00190 · Cited by 82
Maddodi, N., Huang, W., Havighurst, T., Kim, K., Jack Longley, B., & Setaluri, V. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2010.26 · Cited by 80
Herzog, C., Yang, C., Holmes, A., & Kaushal, G. P. (2012) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00659.2011 · Cited by 82
Progress and Challenges in Targeted Protein Degradation for Neurodegenerative Disease Therapy
Fang, Y., Wang, J., Zhao, M., Zheng, Q., Ren, C., Wang, Y., & Zhang, J. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00844 · Cited by 100
Liang, W., Moyzis, A. G., Lampert, M. A., Diao, R. Y., Najor, R. H., & Gustafsson, Å. B. (2020) · Aging Cell · doi:10.1111/acel.13187 · Cited by 80
Critical Role for IL-18 in Spontaneous Lung Inflammation Caused by Autophagy Deficiency
Abdel Fattah, E., Bhattacharya, A., Herron, A., Safdar, Z., & Eissa, N. T. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402277 · Cited by 77
Kravic, B., Harbauer, A. B., Romanello, V., Simeone, L., Vögtle, F.-N., Kaiser, T., Straubinger, M., Huraskin, D., Böttcher, M., Cerqua, C., et al. (2018) · Autophagy · doi:10.1080/15548627.2017.1403716 · Cited by 75
Tan, J. M. J., Mellouk, N., Osborne, S. E., Ammendolia, D. A., Dyer, D. N., Li, R., Brunen, D., van Rijn, J. M., Huang, J., Czuczman, M. A., et al. (2018) · Nature Microbiology · doi:10.1038/s41564-018-0293-5 · Cited by 76
Self-citationSasaki, K., Tsuno, N. H., Sunami, E., Kawai, K., Hongo, K., Hiyoshi, M., Kaneko, M., Murono, K., Tada, N., Nirei, T., et al. (2012) · Anti-Cancer Drugs · doi:10.1097/cad.0b013e328353f8c7 · Cited by 76
Wang, M., Hossain, M. S., Tan, W., Coolman, B., Zhou, J., Liu, S., & Casey, P. J. (2010) · Oncogene · doi:10.1038/onc.2010.247 · Cited by 75
Blocking Autophagy in Oligodendrocytes Limits Functional Recovery after Spinal Cord Injury
Saraswat Ohri, S., Bankston, A. N., Mullins, S. A., Liu, Y., Andres, K. R., Beare, J. E., Howard, R. M., Burke, D. A., Riegler, A. S., Smith, A. E., et al. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.0679-17.2018 · Cited by 70
Reduction of lipid accumulation rescues Bietti's crystalline dystrophy phenotypes
Hata, M., Ikeda, H. O., Iwai, S., Iida, Y., Gotoh, N., Asaka, I., Ikeda, K., Isobe, Y., Hori, A., Nakagawa, S., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1717338115 · Cited by 70
“We also measured p62/SQSTM1 (hereafter, p62) expression to assess autophagic flux (17, 18).”
BackgroundSmith, C. M., Mayer, J. A., & Duncan, I. D. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.0233-13.2013 · Cited by 69
Liu, D., Zhang, Y., Gharavi, R., Park, H. R., Lee, J., Siddiqui, S., Telljohann, R., Nassar, M. R., Cutler, R. G., Becker, K. G., et al. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13176 · Cited by 68
“autophagosome formation, and is thus an autophagosome marker (Kabeya et al. 2000).”
BackgroundVerma, N. K., Conroy, J., Lyons, P. E., Coleman, J., O'Sullivan, M. P., Kornfeld, H., Kelleher, D., & Volkov, Y. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.08.023 · Cited by 68
Simpkins, F., Jang, K., Yoon, H., Hew, K. E., Kim, M., Azzam, D. J., Sun, J., Zhao, D., Ince, T. A., Liu, W., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-3697 · Cited by 67
Overweight in elderly people induces impaired autophagy in skeletal muscle
Potes, Y., de Luxán-Delgado, B., Rodriguez-González, S., Guimarães, M. R. M., Solano, J. J., Fernández-Fernández, M., Bermúdez, M., Boga, J. A., Vega-Naredo, I., & Coto-Montes, A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.05.018 · Cited by 67
Thai, P. N., Seidlmayer, L. K., Miller, C., Ferrero, M., Dorn, G. W., Schaefer, S., Bers, D. M., & Dedkova, E. N. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00382 · Cited by 66
Oncogenic B-RAF Signaling in Melanoma Impairs the Therapeutic Advantage of Autophagy Inhibition
Armstrong, J. L., Corazzari, M., Martin, S., Pagliarini, V., Falasca, L., Hill, D. S., Ellis, N., Al Sabah, S., Redfern, C. P. F., Fimia, G. M., et al. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-3003 · Cited by 65
Comprehensive autophagy evaluation in cardiac disease models
Kaludercic, N., Maiuri, M. C., Kaushik, S., Fernández, Á. F., de Bruijn, J., Castoldi, F., Chen, Y., Ito, J., Mukai, R., Murakawa, T., et al. (2020) · Cardiovascular Research · doi:10.1093/cvr/cvz233 · Cited by 64
Targeted killing of a mammalian cell based upon its specialized metabolic state
Alexander, P. B., Wang, J., & McKnight, S. L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111312108 · Cited by 64
Hosseinzadeh, M., Nikseresht, S., Khodagholi, F., Naderi, N., & Maghsoudi, N. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-015-0703-6 · Cited by 61
The lifecycle of skeletal muscle mitochondria in obesity
Pileggi, C. A., Parmar, G., & Harper, M. (2021) · Obesity Reviews · doi:10.1111/obr.13164 · Cited by 61
The GATOR2 Component Wdr24 Regulates TORC1 Activity and Lysosome Function
Cai, W., Wei, Y., Jarnik, M., Reich, J., & Lilly, M. A. (2016) · PLOS Genetics · doi:10.1371/journal.pgen.1006036 · Cited by 61
Guo, W., Wong, S., Li, M., Liang, W., Liesa, M., Serra, C., Jasuja, R., Bartke, A., Kirkland, J. L., Shirihai, O., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051180 · Cited by 59
Pharmacological modulation of autophagy for Alzheimer's disease therapy: Opportunities and obstacles
Deng, Z., Dong, Y., Zhou, X., Lu, J.-H., & Yue, Z. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.12.009 · Cited by 58
Nazim, U. M., Moon, J.-H., Lee, J.-H., Lee, Y.-J., Seol, J.-W., Eo, S.-K., Lee, J.-H., & Park, S.-Y. (2016) · Oncotarget · doi:10.18632/oncotarget.8048 · Cited by 58
Wang, G.-Y., Bi, Y.-G., Liu, X.-D., Zhao, Y., Han, J.-F., Wei, M., & Zhang, Q.-Y. (2017) · International Journal of Medical Sciences · doi:10.7150/ijms.19800 · Cited by 53
The role of autophagy in brown and beige adipose tissue plasticity
Cairó, M., & Villarroya, J. (2020) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-019-00708-1 · Cited by 53
Drosophila Golgi membrane protein Ema promotes autophagosomal growth and function
Kim, S., Naylor, S. A., & DiAntonio, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1120320109 · Cited by 53
Kwon, C.-Y., Cho, I.-H., & Park, K. S. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01192 · Cited by 52
Sporadic inclusion body myositis: possible pathogenesis inferred from biomarkers.
Weihl, C. C., & Pestronk, A. (2010) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32833d3897 · Cited by 51
Panda, P. K., Fahrner, A., Vats, S., Seranova, E., Sharma, V., Chipara, M., Desai, P., Torresi, J., Rosenstock, T., Kumar, D., et al. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00038 · Cited by 50
A disease causing ATLASTIN 3 mutation affects multiple endoplasmic reticulum-related pathways
Behrendt, L., Kurth, I., & Kaether, C. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03010-x · Cited by 48
Reducing lipofuscin accumulation and cardiomyocytic senescence of aging heart by enhancing autophagy
Li, W.-W., Wang, H.-J., Tan, Y.-Z., Wang, Y.-L., Yu, S.-N., & Li, Z.-H. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112585 · Cited by 47
Li, Q.-Q., Zhang, L., Wan, H.-Y., Liu, M., Li, X., & Tang, H. (2015) · Oncotarget · doi:10.18632/oncotarget.5318 · Cited by 46
Kwon, D. H., Kim, S., Jung, Y. O., Roh, K.-H., Kim, L., Kim, B.-W., Hong, S. B., Lee, I. Y., Song, J. H., Lee, W. C., et al. (2017) · Autophagy · doi:10.1080/15548627.2016.1243199 · Cited by 43
Arnold, C. R., Pritz, T., Brunner, S., Knabb, C., Salvenmoser, W., Holzwarth, B., Thedieck, K., & Grubeck-Loebenstein, B. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.01.018 · Cited by 42
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Kakoty, V., K C, S., Dubey, S. K., Yang, C.-H., & Taliyan, R. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00144 · Cited by 33
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Alghamdi, T. A., Majumder, S., Thieme, K., Batchu, S. N., White, K. E., Liu, Y., Brijmohan, A. S., Bowskill, B. B., Advani, S. L., Woo, M., et al. (2017) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016111208 · Cited by 26
Lei, Y., Zhou, R., Sun, X., Tang, F., Gao, H., Chen, L., & Li, X. (2021) · Annals of Translational Medicine · doi:10.21037/atm-21-6579 · Cited by 22
Demine, S., Tejerina, S., Bihin, B., Thiry, M., Reddy, N., Renard, P., Raes, M., Jadot, M., & Arnould, T. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.25994 · Cited by 21
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“In this study, the Rpt3-deficient mice exhibited an increase in the expression levels of the p62 and LC3 proteins, suggesting the activation of autophagy.”
BackgroundInfluentialMiyatake, S., Hino, K., Natsui, Y., Ebisu, G., & Fujita, S. (2020) · Nutrients · doi:10.3390/nu12092729 · Cited by 7
Metadata
- Authors
- Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T.
- Affiliations
- National Institute for Basic Biology (JP)
- Juntendo University (JP)
- Kansai Medical University (JP)
- Corresponding author
- Yoshimori, Tamotsu
- ORCID
- Mizushima, Noboru
- Venue
- The EMBO Journal
- Published
- 2000-11-01
- Volume
- 19
- Issue
- 21
- Pages
- 5720-5728
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC305793
- OpenAlex
- W1977767269
- Cited by
- 6,605
- References
- 31
- Citations by year
- 2026: 135 · 2025: 173 · 2024: 226 · 2023: 272 · 2022: 287 · 2021: 342 · 2020: 344 · 2019: 380 · 2018: 377 · 2017: 387 · 2016: 381 · 2015: 426 · 2014: 389 · 2013: 447 · 2012: 386
- FWCI
- 18.08
- Type
- journal article
- Language
- en
- Update notices
- erratum (2003-09-01)
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Tokyo Tech Research Repository (Tokyo Institute of Technology) (submittedVersion)
- Funders
- National Institute for Basic Biology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- LC3, autophagy, LC3-II, post-translational processing, C-terminal truncation, autophagosomes, yeast homologue
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Fungal Proteins, HeLa Cells, Humans, Intracellular Membranes, Microtubule-Associated Proteins, Molecular Sequence Data, Phagosomes, Protein Processing, Post-Translational, Subcellular Fractions, Transfection, Microscopy, Immunoelectron, Sequence Homology, Amino Acid, DNA Primers, Rats
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