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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 201–300 of 1,091
Induction of Autophagy during Extracellular Matrix Detachment Promotes Cell Survival
Fung, C., Lock, R., Gao, S., Salas, E., & Debnath, J. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-10-1092 · Cited by 558
Kuma, A., Matsui, M., & Mizushima, N. (2007) · Autophagy · doi:10.4161/auto.4012 · Cited by 555
Self-citationMethods for Monitoring Autophagy from Yeast to Human
Klionsky, D. J., Cuervo, A. M., & Seglen, P. O. (2007) · Autophagy · doi:10.4161/auto.3678 · Cited by 656
Atg8‐family interacting motif crucial for selective autophagy
Noda, N. N., Ohsumi, Y., & Inagaki, F. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.018 · Cited by 553
Self-citationActivation of antibacterial autophagy by NADPH oxidases
Huang, J., Canadien, V., Lam, G. Y., Steinberg, B. E., Dinauer, M. C., Magalhaes, M. A. O., Glogauer, M., Grinstein, S., & Brumell, J. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811045106 · Cited by 556
Allele-selective lowering of mutant HTT protein by HTT–LC3 linker compounds
Li, Z., Wang, C., Wang, Z., Zhu, C., Li, J., Sha, T., Ma, L., Gao, C., Yang, Y., Sun, Y., et al. (2019) · Nature · doi:10.1038/s41586-019-1722-1 · Cited by 551
Autophagy in the Eukaryotic Cell
Reggiori, F., & Klionsky, D. J. (2002) · Eukaryotic Cell · doi:10.1128/ec.01.1.11-21.2002 · Cited by 562
Lithium delays progression of amyotrophic lateral sclerosis
Fornai, F., Longone, P., Cafaro, L., Kastsiuchenka, O., Ferrucci, M., Manca, M. L., Lazzeri, G., Spalloni, A., Bellio, N., Lenzi, P., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708022105 · Cited by 550
Atg8: an autophagy-related ubiquitin-like protein family.
Shpilka, T., Weidberg, H., Pietrokovski, S., & Elazar, Z. (2011) · Genome biology · doi:10.1186/gb-2011-12-7-226 · Cited by 543
“Although mammalian Atg8 proteins were originally implicated in intracellular trafficking processes, they are all found within autophagosomes [73-75].”
BackgroundFader, C. M., Sánchez, D. G., Mestre, M. B., & Colombo, M. I. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.09.011 · Cited by 544
Yoshimoto, K., Hanaoka, H., Sato, S., Kato, T., Tabata, S., Noda, T., & Ohsumi, Y. (2004) · The Plant Cell · doi:10.1105/tpc.104.025395 · Cited by 603
Self-citationAutophagy in thymic epithelium shapes the T-cell repertoire and is essential for tolerance
Nedjic, J., Aichinger, M., Emmerich, J., Mizushima, N., & Klein, L. (2008) · Nature · doi:10.1038/nature07208 · Cited by 552
Self-citationPhosphatidylethanolamine Metabolism in Health and Disease
Calzada, E., Onguka, O., & Claypool, S. M. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.10.001 · Cited by 558
The Molecular Mechanism of Autophagy
Wang, C.-W., & Klionsky, D. J. (2003) · Molecular Medicine · doi:10.1007/bf03402040 · Cited by 543
LC3- and p62-based biochemical methods for the analysis of autophagy progression in mammalian cells
Jiang, P., & Mizushima, N. (2014) · Methods · doi:10.1016/j.ymeth.2014.11.021 · Cited by 534
Self-citationAn Atg4B Mutant Hampers the Lipidation of LC3 Paralogues and Causes Defects in Autophagosome Closure
Fujita, N., Hayashi, M., Fukumoto, H., Omori, H., Yamamoto, A., Noda, T., & Yoshimori, T. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-03-0312 · Cited by 527
Self-citationThe apoptosis/autophagy paradox: autophagic vacuolization before apoptotic death
González‐Polo, R. A., Boya, P., Pauleau, A., Jalil, A., Larochette, N., Souquère, S., Eskelinen, E., Pierron, G., Säftig, P., & Kroemer, G. (2005) · Journal of Cell Science · doi:10.1242/jcs.02447 · Cited by 532
Blocked Autophagy Sensitizes Resistant Carcinoma Cells to Radiation Therapy
Apel, A., Herr, I., Schwarz, H., Rodemann, H. P., & Mayer, A. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-0562 · Cited by 530
Aoki, H., Takada, Y., Kondo, S., Sawaya, R. A., Aggarwal, B. B., & Kondo, Y. (2007) · Molecular Pharmacology · doi:10.1124/mol.106.033167 · Cited by 523
Autophagy delays apoptotic death in breast cancer cells following DNA damage
Abedin, M. J., Wang, D.-P., McDonnell, M. A., Lehmann, U., & Kelekar, A. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402039 · Cited by 532
The Role of Autophagy in Mammalian Development: Cell Makeover Rather than Cell Death
Cecconi, F., & Levine, B. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.08.012 · Cited by 535
Murakawa, T., Yamaguchi, O., Hashimoto, A., Hikoso, S., Takeda, T., Oka, T., Yasui, H., Ueda, H., Akazawa, Y., Nakayama, H., et al. (2015) · Nature Communications · doi:10.1038/ncomms8527 · Cited by 539
Self-citationNew insights into autophagosome–lysosome fusion
Nakamura, S., & Yoshimori, T. (2017) · Journal of Cell Science · doi:10.1242/jcs.196352 · Cited by 540
Self-citationThe dynamic interaction of AMBRA1 with the dynein motor complex regulates mammalian autophagy
Bartolomeo, S. D., Corazzari, M., Nazio, F., Oliverio, S., Lisi, G., Antonioli, M., Pagliarini, V., Matteoni, S., Fuoco, C., Giunta, L., et al. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201002100 · Cited by 561
Colell, A., Ricci, J.-E., Tait, S., Milasta, S., Maurer, U., Bouchier-Hayes, L., Fitzgerald, P., Guio-Carrion, A., Waterhouse, N. J., Li, C. W., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.045 · Cited by 516
Physiological significance of selective degradation of p62 by autophagy
Komatsu, M., & Ichimura, Y. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.017 · Cited by 524
Stimulation of the insulin/mTOR pathway delays cone death in a mouse model of retinitis pigmentosa
Punzo, C., Kornacker, K., & Cepko, C. L. (2008) · Nature Neuroscience · doi:10.1038/nn.2234 · Cited by 515
Polyubiquitin chain-induced p62 phase separation drives autophagic cargo segregation
Sun, D., Wu, R., Zheng, J., Li, P., & Yu, L. (2018) · Cell Research · doi:10.1038/s41422-018-0017-7 · Cited by 521
Snijder, E. J., van der Meer, Y., Zevenhoven-Dobbe, J. C., Onderwater, J. J. M., van der Meulen, J., Koerten, H. K., & Mommaas, A. M. (2006) · Journal of Virology · doi:10.1128/jvi.02501-05 · Cited by 521
Autophagy: a regulated bulk degradation process inside cells
Yoshimori, T. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.07.023 · Cited by 519
Self-citationAutophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages
Kyei, G. B., Dinkins, C., Davis, A. S., Roberts, E., Singh, S. B., Dong, C., Wu, L., Kominami, E., Ueno, T., Yamamoto, A., et al. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200903070 · Cited by 509
Self-citationA block of autophagy in lysosomal storage disorders
Settembre, C., Fraldi, A., Jahreiss, L., Spampanato, C., Venturi, C. B., Medina, D. L., de Pablo, R., Tacchetti, C., Rubinsztein, D. C., & Ballabio, A. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm289 · Cited by 509
Tong, Y., Yamaguchi, H., Giaime, E., Boyle, S., Kopan, R., Kelleher, R. J., & Shen, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004676107 · Cited by 521
Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome
Morselli, E., Mariño, G., Bennetzen, M. V., Eisenberg, T., Megalou, E. V., Schroeder, S., Cabrera, S., Bénit, P., Rustin, P., Criollo, A., et al. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201008167 · Cited by 509
Vitamin D Is Required for IFN-γ–Mediated Antimicrobial Activity of Human Macrophages
Fabri, M., Stenger, S., Shin, D., Yuk, J., Liu, P. T., Realegeno, S. E., Lee, H. M., Krutzik, S. R., Schenk, M., Sieling, P. A., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3003045 · Cited by 517
Autophagy in chronically ischemic myocardium
Yan, L., Vatner, D. E., Kim, S.-J., Ge, H., Masurekar, M., Massover, W. H., Yang, G., Matsui, Y., Sadoshima, J., & Vatner, S. F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506843102 · Cited by 430
Amm, I., Sommer, T., & Wolf, D. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.031 · Cited by 509
Mechanisms of Autophagosome Biogenesis
Rubinsztein, D. C., Shpilka, T., & Elazar, Z. (2012) · Current Biology · doi:10.1016/j.cub.2011.11.034 · Cited by 517
Role of autophagy in G2019S‐LRRK2‐associated neurite shortening in differentiated SH‐SY5Y cells
Plowey, E. D., Cherra, S. J., Liu, Y., & Chu, C. T. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05217.x · Cited by 517
Autophagosome Formation and Molecular Mechanism of Autophagy
Tanida, I. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3482 · Cited by 505
Rusten, T. E., Lindmo, K., Juhász, G., Sass, M., Seglen, P. O., Brech, A., & Stenmark, H. (2004) · Developmental Cell · doi:10.1016/j.devcel.2004.07.005 · Cited by 487
Overview of macroautophagy regulation in mammalian cells
Mehrpour, M., Esclatine, A., Beau, I., & Codogno, P. (2010) · Cell Research · doi:10.1038/cr.2010.82 · Cited by 516
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 504
Zavodszky, E., Seaman, M. N. J., Moreau, K., Jimenez-Sanchez, M., Breusegem, S. Y., Harbour, M. E., & Rubinsztein, D. C. (2014) · Nature Communications · doi:10.1038/ncomms4828 · Cited by 466
Inhibition of Autophagy Prevents Hippocampal Pyramidal Neuron Death after Hypoxic-Ischemic Injury
Koike, M., Shibata, M., Tadakoshi, M., Gotoh, K., Komatsu, M., Waguri, S., Kawahara, N., Kuida, K., Nagata, S., Kominami, E., et al. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.070876 · Cited by 486
Self-citationDifferential Effects of Endoplasmic Reticulum Stress-induced Autophagy on Cell Survival
Ding, W., Ni, H., Gao, W., Hou, Y., Melan, M. A., Chen, X., Stolz, D. B., Shao, Z.-M., & Yin, X. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609267200 · Cited by 494
The ATG conjugation systems are important for degradation of the inner autophagosomal membrane
Tsuboyama, K., Koyama-Honda, I., Sakamaki, Y., Koike, M., Morishita, H., & Mizushima, N. (2016) · Science · doi:10.1126/science.aaf6136 · Cited by 485
Self-citationApoptosis blocks Beclin 1-dependent autophagosome synthesis: an effect rescued by Bcl-xL
Luo, S., & Rubinsztein, D. C. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.121 · Cited by 495
Kubli, D. A., Zhang, X., Lee, Y., Hanna, R. A., Quinsay, M. N., Nguyen, C. K., Jimenez, R., Petrosyan, S., Murphy, A. N., & Gustafsson, Å. B. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.411363 · Cited by 476
Inbal, B., Bialik, S., Sabanay, I., Shani, G., & Kimchi, A. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200109094 · Cited by 481
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Dreux, M., Gastaminza, P., Wieland, S. F., & Chisari, F. V. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907344106 · Cited by 500
Sou, Y., Waguri, S., Iwata, J.-I., Ueno, T., Fujimura, T., Hara, T., Sawada, N., Yamada, A., Mizushima, N., Uchiyama, Y., et al. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-03-0309 · Cited by 485
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Wang, K., Liu, C.-Y., Zhou, L.-Y., Wang, J.-X., Wang, M., Zhao, B., Zhao, W.-K., Xu, S.-J., Fan, L.-H., Zhang, X.-J., et al. (2015) · Nature Communications · doi:10.1038/ncomms7779 · Cited by 473
The Legionella Effector RavZ Inhibits Host Autophagy Through Irreversible Atg8 Deconjugation
Choy, A., Dancourt, J., Mugo, B., O’Connor, T. J., Isberg, R. R., Melia, T. J., & Roy, C. R. (2012) · Science · doi:10.1126/science.1227026 · Cited by 473
Enhancing Macroautophagy Protects against Ischemia/Reperfusion Injury in Cardiac Myocytes
Hamacher-Brady, A., Brady, N. R., & Gottlieb, R. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603783200 · Cited by 555
TRAF6 and A20 Regulate Lysine 63–Linked Ubiquitination of Beclin-1 to Control TLR4-Induced Autophagy
Shi, C.-S., & Kehrl, J. H. (2010) · Science Signaling · doi:10.1126/scisignal.2000751 · Cited by 481
Autophagy Is an Essential Component of Drosophila Immunity against Vesicular Stomatitis Virus
Shelly, S. S., Lukinova, N. I., Bambina, S., Berman, A., & Cherry, S. R. (2009) · Immunity · doi:10.1016/j.immuni.2009.02.009 · Cited by 489
Lee, S., Satō, Y., & Nixon, R. A. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6412-10.2011 · Cited by 478
Small molecule regulators of autophagy identified by an image-based high-throughput screen
Zhang, L., Yu, J., Pan, H., Hu, P., Yan, H., Cai, W., Zhu, H., Yu, A. D., Xie, X., Ma, D., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709695104 · Cited by 470
Fader, C. M., Sánchez‐Martínez, D., Furlán, M., & Colombo, M. I. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00677.x · Cited by 490
siRNA Screening of the Kinome Identifies ULK1 as a Multidomain Modulator of Autophagy
Chan, E. Y. W., Kir, S., & Tooze, S. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703663200 · Cited by 422
Autophagy Protects the Proximal Tubule from Degeneration and Acute Ischemic Injury
Kimura, T., Takabatake, Y., Takahashi, A., Kaimori, J.-Y., Matsui, I., Namba, T., Kitamura, H., Niimura, F., Matsusaka, T., Soga, T., et al. (2011) · Journal of the American Society of Nephrology · doi:10.1681/asn.2010070705 · Cited by 461
The tumor suppressor gene ARHI regulates autophagy and tumor dormancy in human ovarian cancer cells
Lü, Z., Luo, R. Z.-T., Lu, Y., Zhang, X., Yu, Q., Khare, S., Kondo, S., Kondo, Y., Yu, Y., Mills, G. B., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci35512 · Cited by 466
A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth
Kim, S., Wong, P., & Coulombe, P. A. (2006) · Nature · doi:10.1038/nature04659 · Cited by 463
T Helper 2 Cytokines Inhibit Autophagic Control of Intracellular Mycobacterium tuberculosis
Harris, J., Haro, S. A. D., Master, S. S., Keane, J., Roberts, E. A., Delgado, M. A., & Deretic, V. P. (2007) · Immunity · doi:10.1016/j.immuni.2007.07.022 · Cited by 471
Woldt, E., Sebti, Y., Solt, L. A., Duhem, C., Lancel, S., Eeckhoute, J., Hesselink, M. K. C., Paquet, C., Delhaye, S., Shin, Y., et al. (2013) · Nature Medicine · doi:10.1038/nm.3213 · Cited by 467
Dynein mutations impair autophagic clearance of aggregate-prone proteins
Ravikumar, B., Acevedo-Arozena, A., Imarisio, S., Berger, Z., Vacher, C., O'Kane, C. J., Brown, S. D. M., & Rubinsztein, D. C. (2005) · Nature Genetics · doi:10.1038/ng1591 · Cited by 416
Florey, O., Kim, S. E., Sandoval, C. P., Haynes, C. M., & Overholtzer, M. (2011) · Nature Cell Biology · doi:10.1038/ncb2363 · Cited by 459
English, L., Chemali, M., Duron, J., Rondeau, C., Laplante, A., Gingras, D., Alexander, D., Leib, D. A., Norbury, C. C., Lippé, R., et al. (2009) · Nature Immunology · doi:10.1038/ni.1720 · Cited by 482
Egr-1 Regulates Autophagy in Cigarette Smoke-Induced Chronic Obstructive Pulmonary Disease
Chen, Z.-H., Kim, H. P., Sciurba, F. C., Lee, S.-J., Feghali-Bostwick, C., Stolz, D. B., Dhir, R., Landreneau, R. J., Schuchert, M. J., Yousem, S. A., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003316 · Cited by 459
Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1
Shibata, M., Lu, T., Furuya, T., Degterev, A., Mizushima, N., Yoshimori, T., MacDonald, M., Yankner, B., & Yuan, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600364200 · Cited by 458
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Caramés, B., Hasegawa, A., Taniguchi, N., Miyaki, S., Blanco, F. J., & Lotz, M. (2011) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2011-200557 · Cited by 466
Effects of Sex, Strain, and Energy Intake on Hallmarks of Aging in Mice
Mitchell, S. J., Madrigal-Matute, J., Scheibye-Knudsen, M., Fang, E., Aon, M., González-Reyes, J. A., Cortassa, S., Kaushik, S., Gonzalez-Freire, M., Patel, B., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.027 · Cited by 451
“Analysis of steady-state levels of LC3-II, the most commonly used marker to measure autophagic compartments (Kabeya et al., 2000), revealed that 40% CR significantly increased levels of LC3-II in B6 mice when compared to 20% CR (Figures 5E and 5F).”
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Matsunaga, K., Morita, E., Saitoh, T., Akira, S., Ktistakis, N. T., Izumi, T., Noda, T., & Yoshimori, T. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911141 · Cited by 456
Self-citationStingele, S., Stoehr, G., Peplowska, K., Cox, J., Mann, M., & Storchova, Z. (2012) · Molecular Systems Biology · doi:10.1038/msb.2012.40 · Cited by 468
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Jia, J., Claude-Taupin, A., Gu, Y., Choi, S. W., Peters, R., Bissa, B., Mudd, M. H., Allers, L., Pallikkuth, S., Lidke, K. A., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2019.10.025 · Cited by 434
The Itinerary of Autophagosomes: From Peripheral Formation to Kiss‐and‐Run Fusion with Lysosomes
Jahreiss, L., Menzies, F. M., & Rubinsztein, D. C. (2008) · Traffic · doi:10.1111/j.1600-0854.2008.00701.x · Cited by 490
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Zhu, J.-H., Horbinski, C., Guo, F., Watkins, S. C., Uchiyama, Y., & Chu, C. T. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.060524 · Cited by 447
Ge, L., Melville, D., Zhang, M., & Schekman, R. W. (2013) · eLife · doi:10.7554/elife.00947 · Cited by 450
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Lira, V. A., Okutsu, M., Zhang, M., Greene, N. P., Laker, R. C., Breen, D. S., Hoehn, K. L., & Yan, Z. (2013) · The FASEB Journal · doi:10.1096/fj.13-228486 · Cited by 432
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Self-citation
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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