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Molecular dissection of autophagy: two ubiquitin-like systems
Abstract
Recent analyses of the genes required for autophagy--intracellular bulk protein degradation--in yeast have revealed two ubiquitin-like systems, both of which are involved in the membrane dynamics of the process. Molecular dissection of these systems is now revealing some surprises.
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“One universal activator of autophagy is a decrease in nutrient availability and this stimulation occurs, at least in part, by the inhibition of TOR (target of rapamycin) signalling 74 .”
From The common biology of cancer and ageing (2007) · cites this paper as [74]
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Cites
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605
Self-citationAutophagy as a Regulated Pathway of Cellular Degradation
Klionsky, D. J., & Emr, S. D. (2000) · Science · doi:10.1126/science.290.5497.1717 · Cited by 3,630
A ubiquitin-like system mediates protein lipidation
Ichimura, Y., Kirisako, T., Takao, T., Satomi, Y., Shimonishi, Y., Ishihara, N., Mizushima, N., Tanida, I., Kominami, E., Ohsumi, M., et al. (2000) · Nature · doi:10.1038/35044114 · Cited by 2,139
Self-citationIsolation 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-citationDissection of Autophagosome Formation Using Apg5-Deficient Mouse Embryonic Stem Cells
Mizushima, N., Yamamoto, A., Hatano, M., Kobayashi, Y., Kabeya, Y., Suzuki, K., Tokuhisa, T., Ohsumi, Y., & Yoshimori, T. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.4.657 · Cited by 1,361
Self-citationAutophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction.
Takeshige, K., Baba, M., Tsuboi, S., Noda, T., & Ohsumi, Y. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.119.2.301 · Cited by 1,266
Self-citationTor-Mediated Induction of Autophagy via an Apg1 Protein Kinase Complex
Kamada, Y., Funakoshi, T., Shintani, T., Nagano, K., Ohsumi, M., & Ohsumi, Y. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.6.1507 · Cited by 1,145
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
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Diversity of Signaling Controls of Macroautophagy in Mammalian Cells.
Petiot, A., Pattingre, S., Arico, S., Meley, D., & Codogno, P. (2002) · Cell Structure and Function · doi:10.1247/csf.27.431 · Cited by 68
Structure of Ubiquitin-fold Modifier 1-specific Protease UfSP2
Ha, B. H., Jeon, Y. J., Shin, S. C., Tatsumi, K., Komatsu, M., Tanaka, K., Watson, C. M., Wallis, G. A., Chung, C. H., & Kim, E. E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.172171 · Cited by 67
Role of autophagy in alcohol and drug-induced liver injury
Williams, J. A. R., & Ding, W. (2019) · Food and Chemical Toxicology · doi:10.1016/j.fct.2019.111075 · Cited by 66
“LC3-II is stable on the autophagosome membrane and is commonly used as a marker for autophagy activation (Ichimura et al., 2000; Kabeya et al., 2000; Ohsumi, 2001; Yoshii and Mizushima, 2017).”
BackgroundSalete-Granado, D., Carbonell, C., Puertas-Miranda, D., Vega-Rodríguez, V.-J., Macia, M. G., Herrero, A. B., & Marcos, M. (2023) · Antioxidants · doi:10.3390/antiox12071425 · Cited by 69
“Finally, the Atg12–Atg5–Atg16 complex conjugates LC3-I with phosphatidylethanolamine to form LC3-II [194,195], which, together with p62 and other cargo receptors, is indispensable for the selectivity of autophagy [196].”
BackgroundInfluentialKwon, S. I., & Park, O. K. (2008) · Journal of Plant Biology · doi:10.1007/bf03036132 · Cited by 68
“Two ubiquitin-like conjugation pathways are involved in the elongation of autophagic vesicles (Ohsumi, 2001; Klionsky, 2005; Thompson and Vierstra, 2005).”
BackgroundInfluentialSimonsen, A., Cumming, R. C., Lindmo, K., Galaviz, V., Cheng, S., Rusten, T. E., & Finley, K. D. (2007) · Genetics · doi:10.1534/genetics.106.065011 · Cited by 67
“Atg8/LC3 remains bound to autophagic membranes until degradation in lysosomes, thus serving as a useful marker of autophagy (Ohsumi 2001).”
BackgroundGSA11 Encodes a Unique 208-kDa Protein Required for Pexophagy and Autophagy in Pichia pastoris
STRØMHAUG, P. E., Bevan, A., & Dunn, W. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104087200 · Cited by 67
Rothe, K., Porter, V., & Jiang, X. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030461 · Cited by 67
“ATG16L1 binds to ATG5 and then ATG16L1 dimerizes with another ATG12-ATG5-ATG16L1 complex, followed by attachment to the phagophore membrane [22].”
BackgroundInfluentialRole of autophagy during plant-virus interactions
Ismayil, A., Yang, M., & Liu, Y. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.07.001 · Cited by 66
Luckhart, S., Giulivi, C., Drexler, A., Antonova‐Koch, Y., Sakaguchi, D., Napoli, E., Wong, S., Price, M. S., Eigenheer, R. A., Phinney, B. S., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003180 · Cited by 68
Pineapple bromelain induces autophagy, facilitating apoptotic response in mammary carcinoma cells
Bhui, K., Tyagi, S., Prakash, B., & Shukla, Y. (2010) · BioFactors · doi:10.1002/biof.121 · Cited by 66
Nuclear DNA degradation during heterokaryon incompatibility in Neurospora crassa
Marek, S. M., Wu, J. D., Glass, N. L., Gilchrist, D. G., & Bostock, R. M. (2003) · Fungal Genetics and Biology · doi:10.1016/s1087-1845(03)00086-0 · Cited by 66
Wang, L., Wang, J., Xiong, H., Wu, F., Lan, T., Zhang, Y., Guo, X., Wang, H., Saleem, M., Jiang, C., et al. (2016) · EBioMedicine · doi:10.1016/j.ebiom.2016.03.022 · Cited by 66
“autophagy essential genes (Ohsumi, 2001), such as ATG5, ATG7 and BECLIN1, were effectively depleted by shRNAs, 2-DG treatment significantly induced prostate cancer cell apoptosis, as demonstrated by the increase of cleaved PARP levels, and a 45% or greater reduction of cell viability (Fig.”
Mechanisms of CD4 T-cell depletion triggered by HIV-1 viral proteins.
Varbanov, M., Espert, L., & Biard‐Piechaczyk, M. (2006) · PubMed · Cited by 66
Autophagy Contributes to the Quality Control of Leaf Mitochondria
Nakamura, S., Hagihara, S., Otomo, K., Ishida, H., Hidema, J., Nemoto, T., & Izumi, M. (2020) · Plant and Cell Physiology · doi:10.1093/pcp/pcaa162 · Cited by 69
“UVB damage increases the association of autophagic membranes with mitochondria The ATG8 ubiquitin-like protein family is an integral component of autophagosomal membranes (Ohsumi 2001).”
BackgroundInfluentialNeuronal autophagy in cerebral ischemia
Xu, F., Gu, J., & Qin, Z. (2012) · Neuroscience Bulletin · doi:10.1007/s12264-012-1268-9 · Cited by 66
“3 Vesicle expansion and completion Two ubiquitinlike conjugation systems, the Atg12-Atg5-Atg16L1 complex and the LC3 (Atg8 homolog)-phosphatidylethanolamine (PE) conjugate, play important roles in vesicle expansion and completion([44,45]).”
BackgroundAutophagy in aging and in neurodegenerative disorders
Rajawat, Y. S., & Bossis, I. (2008) · HORMONES · doi:10.14310/horm.2002.1111037 · Cited by 66
Multifunction of autophagy-related genes in filamentous fungi
Khan, I. A., Lu, J., Liu, X., Rehman, A., & Lin, F. (2012) · Microbiological Research · doi:10.1016/j.micres.2012.01.004 · Cited by 65
MUBs, a Family of Ubiquitin-fold Proteins That Are Plasma Membrane-anchored by Prenylation
Downes, B. P., Saracco, S. A., Lee, S. S., Crowell, D. N., & Vierstra, R. D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602283200 · Cited by 67
BECN1-dependent CASP2 incomplete autophagy induction by binding to rabies virus phosphoprotein
Liu, J., Wang, H., Gu, J., Deng, T., Yuan, Z.-C., Hu, B., Xu, Y., Yan, Y., Zan, J., Liao, M., et al. (2017) · Autophagy · doi:10.1080/15548627.2017.1280220 · Cited by 66
“have been shown to mediate the formation of the autophagosome.(8) These systems are required for the elongation and”
BackgroundProgrammed cell death in cardiac myocytes: strategies to maximize post-ischemic salvage
Mani, K. M. (2008) · Heart Failure Reviews · doi:10.1007/s10741-007-9073-7 · Cited by 64
Shimanuki, M., Chung, S., Chikashige, Y., Kawasaki, Y., Uehara, L., Tsutsumi, C., Hatanaka, M., Hiraoka, Y., Nagao, K., & Yanagida, M. (2007) · Genes to Cells · doi:10.1111/j.1365-2443.2007.01079.x · Cited by 62
“The levels of each of the ~25 transcripts of autophagy (Ohsumi 2001; Nakashima et al. 2006; Kohda et al. 2007) and wtf (the pseudo genes containing a retrotransposon sequence; Wood et al.”
BackgroundIntertwined pathways of programmed cell death in immunity
Hedrick, S. Μ., Ch’en, I. L., & Alves, B. N. (2010) · Immunological Reviews · doi:10.1111/j.1600-065x.2010.00918.x · Cited by 66
Zhao, T., Mao, L., Yu, Z., Hui, Y., Feng, H., Wang, X., Lin, L., Fan, X., Chen, X., Wang, B., et al. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.107308 · Cited by 63
CD36 and LC3B initiated autophagy in B cells regulates the humoral immune response
He, C., Wang, S., Zhou, C., He, M., Wang, J., Ladds, M. J. G. W., Lianoudaki, D., Sedimbi, S. K., Lane, D. P., Westerberg, L. S., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1885183 · Cited by 65
“Next, via a variety of ubiquitinlike reactions, LC3B-I becomes conjugated the lipid phosphatidylethanolamine to generate LC3B-II which is involved in autophagosome membrane expansion and fusion [37,38].”
BackgroundAutophagic elimination of ribosomes during spermiogenesis provides energy for flagellar motility
Lei, Y., Zhang, X., Xu, Q., Liu, S., Li, C., Jiang, H., Lin, H., Kong, E., Liu, J., Qi, S., et al. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.07.015 · Cited by 65
Voigt, O., & Pöggeler, S. (2013) · Autophagy · doi:10.4161/auto.22398 · Cited by 60
Zhang, J., Ahmad, S., Wang, L., Han, Q., Zhang, J., & Luo, Y. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.04.021 · Cited by 63
Autophagy sustains the replication of porcine reproductive and respiratory virus in host cells
Liu, Q., Qin, Y., Zhou, L., Kou, Q., Guo, X., Ge, X., Yang, H., & Hu, H. (2012) · Virology · doi:10.1016/j.virol.2012.03.022 · Cited by 63
“Scale bars in of autophagosome, therefore silencing LC3 will specifically block the autophagy pathway (Klionsky et al., 2008; Ohsumi, 2001).”
InfluentialCecconi, F., Piacentini, M., & Fimia, G. M. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.64 · Cited by 63
Autophagy in plant pathogenic fungi
Liu, X., Xu, F., Snyder, J. H., Shi, H., Lu, J., & Lin, F. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.03.022 · Cited by 62
Zhang, H., Dong, X., Zhao, R., Zhang, R., Xu, C., Wang, X., Liu, C., Hu, X., Huang, S., & Chen, L. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.12.008 · Cited by 63
“LC3 is conjugated to phosphatidylethanolamine (PE) through an enzymatic cascade involving ATG7 (as an E1-like enzyme), ATG3 (as an E2-like enzyme) and ATG5-12-16 complex, and and is located on autophagosomal membranes after posttranslational modifications [18; 21; 22].”
BackgroundMicroautophagy in Plants: Consideration of Its Molecular Mechanism
Sieńko, K., Poormassalehgoo, A., Yamada, K., & Goto‐Yamada, S. (2020) · Cells · doi:10.3390/cells9040887 · Cited by 63
“Macroautophagy is the most well-studied type of autophagy, and more than 40 autophagy-related (ATG) proteins have been identified as contributing to macroautophagy in various eukaryotes [4,7,8].”
BackgroundManley, S., Ni, H., Williams, J. A. R., Kong, B., DiTacchio, L., Guo, G. L., & Ding, W. (2014) · Redox Biology · doi:10.1016/j.redox.2014.08.007 · Cited by 61
“Furthermore, we found that ethanol treatment had decreased expression of various essential autophagy genes and several other FoxO3 target genes in FXR KO mice compared with wild type mice.”
BackgroundHan, C., Sun, B., Wang, W., Cai, W., Lou, D. W., Sun, Y. K., & Zhao, X. (2011) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.223.243 · Cited by 61
“However, it is contrary to the result in breast carcinoma cells in which the expression of beclin-1 is decreased (Ohsumi 2001).”
BackgroundResultTargeting MKK3 as a novel anticancer strategy: molecular mechanisms and therapeutical implications
Baldari, S., Ubertini, V., Garufi, A., D’Orazi, G., & Bossi, G. (2015) · Cell Death and Disease · doi:10.1038/cddis.2014.591 · Cited by 59
An ER-Localized SNARE Protein Is Exported in Specific COPII Vesicles for Autophagosome Biogenesis
Lemus, L., Ribas, J., Sikorska, N., & Goder, V. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.01.047 · Cited by 60
“A structure called ‘‘phagophore’’ forms in the cytosol at phagophore assembly sites (PAS), elongates while engulfing cytosolic material, and closes to form a double membrane-layered autophagosome that fuses with the vacuole/lysosome for material recycling (Klionsky, 2007; Ohsumi, 2001).”
BackgroundAdvances in indole-containing alkaloids as potential anticancer agents by regulating autophagy
Luo, M.-L., Huang, W., Zhu, H.-P., Peng, C. Y., Zhao, Q., & Han, B. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112827 · Cited by 63
Sasaki, M., Miyakoshi, M., Sato, Y., & Nakanuma, Y. (2011) · Liver International · doi:10.1111/j.1478-3231.2011.02656.x · Cited by 59
“Autophagy in human diseases has been highlighted during the last decade (1, 2, 5) and recent data demonstrated that autophagy is involved in major field of hepatology (6–12).”
BackgroundThe plasma membrane brings autophagosomes to life
Cuervo, A. M. (2010) · Nature Cell Biology · doi:10.1038/ncb0810-735 · Cited by 59
Atg19p Ubiquitination and the Cytoplasm to Vacuole Trafficking Pathway in Yeast
Baxter, B. K., Abeliovich, H., Zhang, X., Stirling, A. G., Burlingame, A. L., & Goldfarb, D. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508064200 · Cited by 59
Autophagy, and BiP level decrease are early key events in retrograde degeneration of motoneurons
Penas, C., Font-Nieves, M., Forés, J., Petegnief, V, Planas, A., Navarro, X., & Casas, C. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.24 · Cited by 58
Imoto, Y., Yoshida, Y., Yagisawa, F., Kuroiwa, H., & Kuroiwa, T. (2011) · Microscopy · doi:10.1093/jmicro/dfr034 · Cited by 59
Interplay between the cellular autophagy machinery and positive-stranded RNA viruses
Shi, J., & Luo, H. (2012) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gms010 · Cited by 59
“Atg12 finally forms a conjugate with Atg5 to activate the formation of autophagosomes [22] .”
BackgroundThe Ubiquitin System and Jasmonate Signaling
Durand, A. N., Pauwels, L., & Goossens, A. (2016) · Plants · doi:10.3390/plants5010006 · Cited by 57
“[51–53].”
AMPK promotes tolerance to Ras pathway inhibition by activating autophagy
Sanduja, S., Feng, Y., Mathis, R. A., Sokol, E. S., Reinhardt, F., Halaban, R., & Gupta, P. B. (2016) · Oncogene · doi:10.1038/onc.2016.70 · Cited by 59
“One such catabolic process is autophagy (20, 21, 26), a ‘self-eating’ program in which cells engulf and break down their organelles and cytoplasmic proteins to generate energy.”
BackgroundUchimura, Y., Nakao, M., & Saitoh, H. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00321-7 · Cited by 59
Unique Role for the UbL-UbA Protein Ddi1 in Turnover of SCFUfo1 Complexes
Ivantsiv, Y., Kaplun, L., Tzirkin, R., Shabek, N., & Raveh, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.5.1579-1588.2006 · Cited by 58
“We did not find a requirement for Rsp5 for degradation of Ufo1 and also no requirement for the autophagy pathway which is inhibited in atg7 mutants (33) (Fig.”
BackgroundRegulation of Chlorophagy during Photoinhibition and Senescence: Lessons from Mitophagy
Nakamura, S., & Izumi, M. (2018) · Plant and Cell Physiology · doi:10.1093/pcp/pcy096 · Cited by 59
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Zhang, C., Wang, J., Pan, Z., Wang, S., Zhang, L., Wang, Q., Ye, Q., Zhou, A., Xie, S., Zeng, F., et al. (2021) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2021.04.010 · Cited by 57
Seiliez, I., Gabillard, J., Riflade, M., Sadoul, B. C., Dias, K., Avérous, J., Tesseraud, S., Skiba, S., & Panserat, S. (2012) · Autophagy · doi:10.4161/auto.18863 · Cited by 65
Hanada, T., Satomi, Y., Takao, T., & Ohsumi, Y. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.03.009 · Cited by 57
“Formation of autophagosomes requires two ubiquitin-like conjugation systems [1].”
BackgroundSelf-citationDifferential Function of the Two Atg4 Homologues in the Aggrephagy Pathway in Caenorhabditis elegans
Wu, F., Li, Y., Wang, F., Noda, N. N., & Zhang, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.365676 · Cited by 59
“Among the core autophagic machinery, two ubiquitin-like systems, theAtg8 systemand theAtg12 system, are essential for the expansion and closure of the autophagosome (1, 3).”
BackgroundDröge, W., & Kinscherf, R. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1953 · Cited by 58
“(44, 136, 183), and elicit the phosphorylation and inhibition of”
Lippai, M., Csikós, G., Maróy, P., Lukácsovich, T., Juhász, G., & Sass, M. (2008) · Autophagy · doi:10.4161/auto.5719 · Cited by 56
Targeting regulated cell death in aortic aneurysm and dissection therapy
Chen, Y., He, Y., Wei, X., & Jiang, D. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.106048 · Cited by 59
The emerging role of autophagy in plant pathogen attack and host defence
Talbot, N. J., & Kershaw, M. J. (2009) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2009.05.008 · Cited by 59
Zhang, L. R., Yao, Z., & Ji, G. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01459 · Cited by 56
“Although being used initially as empirical prescription for Frontiers in Pharmacology | www.frontiersin.org 1 December 2018 | Volume 9 | Article 1459 individuals, some of HM has been supported by clinical evidence in the treatment of NAFLD (Pan et al., 2013; Yu et al., 2015).”
MethodPattingre, S., Petiot, A., & Codogno, P. (2004) · Methods in Enzymology · doi:10.1016/s0076-6879(04)90002-x · Cited by 46
Alvero, A. B., Montagna, M. K., Chen, R., Kim, K. H., Kyungjin, K., Visintin, I., Fu, H., Brown, D., & Mor, G. (2009) · Cancer · doi:10.1002/cncr.24397 · Cited by 55
Plant Autophagy: An Intricate Process Controlled by Various Signaling Pathways
Wang, P., Wang, T., Han, J., Li, M., Zhao, Y., Su, T., & Ma, C. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.754982 · Cited by 55
“Simultaneously, ATG8phosphatidylethanolamine (PE) is inserted into the membrane of the expanding phagophore via a ubiquitin-like conjugation pathway (Ohsumi, 2001; Minina et al., 2018).”
BackgroundGarrido‐Maraver, J., Paz, M. V., Cordero, M. D., Lorite, J. B., Oropesa-Ávila, M., de la Mata, M., Pavón, A. D., de Lavera, I., Alcocer‐Gómez, E., Galán, F., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.027 · Cited by 58
Drosophila as a model system to study autophagy
Zirin, J. D., & Perrimon, N. (2010) · Seminars in Immunopathology · doi:10.1007/s00281-010-0223-y · Cited by 56
“Vesicle expansion is mediated by two ubiquitin-like groups, Atg5–Atg12–Atg16, and Atg8, both of which are highly conserved from yeast to mammals [84].”
BackgroundAutophagy protein 16-mediated autophagy is required for the encystation of Acanthamoeba castellanii
Song, S.-M., Han, B.-I., Moon, E., Lee, Y., Yu, H. S., Jha, B. K., Danne, D.-B. S., Kong, H.-H., Chung, D.-I., & Hong, Y. (2012) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2012.02.013 · Cited by 55
Macroautophagy and its role in nutrient homeostasis
Stipanuk, M. H. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.2009.00252.x · Cited by 56
Salah, F. S., Ebbinghaus, M., Muley, V. Y., Zhou, Z., Al-Saadi, K. R., Pacyna-Gengelbach, M., O’Sullivan, G. A., Betz, H., König, R., Wang, Z.-Q., et al. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.93 · Cited by 56
“Thus GABARAP deficiency promoted cellular death after genotoxic stress by DMBA, which is consistent with the role of its homolog Atg8 in yeast and the concept that autophagy blockade may enhance cellular death under stress conditions.(7,12) The immune response has an essential role in delineating tumor outgrowth and p…”
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Esfahani, A. H., Sverchkova, A., Sáez-Rodríguez, J., Schuppert, A., & Brehme, M. (2018) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005890 · Cited by 60
“…folding and quality control (Hartl and Hayer-Hartl 2002, Young et al. 2004, Hartl et al. 2011, Kim et al. 2013), clearance through autophagy (Ohsumi 2001, Behrends et al. 2010, Janku et al. 2011, Rubinsztein et al. 2012, Türei et al. 2015) and the ubiquitin-proteasome system (UPS) (McNaught…”
BackgroundAutophagy in Alcohol-Induced Multiorgan Injury: Mechanisms and Potential Therapeutic Targets
Li, Y., Wang, S., Ni, H., Huang, H., & Ding, W. (2014) · BioMed Research International · doi:10.1155/2014/498491 · Cited by 55
Porcine circovirus type 2 explores the autophagic machinery for replication in PK-15 cells
Zhu, B., Xu, F., Li, J., Shuai, J., Li, X., & Fang, W. (2011) · Virus Research · doi:10.1016/j.virusres.2011.11.012 · Cited by 54
Liang, C., Li, H., Zhou, H., Zhang, S., Liu, Z., Zhou, Q., & Sun, F. (2011) · Oncology Reports · doi:10.3892/or.2011.1593 · Cited by 57
“Fujita et al (5) used dystrophy-associated fer-1-like protein (dysferlin) degradation to investigate two ERAD models and found that when misfolded dysferlin aggregated on the ER membrane excessively, the cell chose the autophagy/lysosome ERAD system rather than the ubiquitin/proteasome (6,7).”
Oh, S., & Roh, C. (2017) · Obstetrics & Gynecology Science · doi:10.5468/ogs.2017.60.3.241 · Cited by 53
“Autophagosome elongation occurs via two ubiquitin-like conjugation systems, the Atg5-Atg12 conjugation system and the LC3 (the mammalian homolog of yeast Atg8) conjugation system [18].”
BackgroundShangguan, L., Fang, X., Chen, L., Cui, L., & Fang, J. (2018) · Planta · doi:10.1007/s00425-018-2864-3 · Cited by 54
“Autophagy-Related Genes (ARGs) were first reported in yeast, and more than 30 ARGs have been identified to date (Ohsumi 2001; Nakatogawa et al. 2007).”
BackgroundMulti-Modal Biological Destruction by Cold Atmospheric Plasma: Capability and Mechanism
Yan, D., Malyavko, A., Wang, Q., Ostrikov, K., Sherman, J. H., & Keidar, M. (2021) · Biomedicines · doi:10.3390/biomedicines9091259 · Cited by 55
Yoshimura, K., Shibata, M., Koike, M., Gotoh, K., Fukaya, M., Watanabe, M., & Uchiyama, Y. (2006) · Autophagy · doi:10.4161/auto.2744 · Cited by 53
Hilgert, N., Huentelman, M. J., Thorburn, A. Q., Fransén, E., Dieltjens, N., Mueller‐Malesińska, M., Pollak, A., Skórka, A., Waligora, J., Płoski, R., et al. (2008) · European Journal of Human Genetics · doi:10.1038/ejhg.2008.201 · Cited by 53
Wei, C., Chang, C., & Liao, V. H. (2017) · Phytomedicine · doi:10.1016/j.phymed.2017.09.002 · Cited by 54
Osawa, T., Shimamura, T., Saito, K., Hasegawa, Y., Ishii, N., Nishida, M., Ando, R., Kondo, A., Anwar, M., Tsuchida, R., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.087 · Cited by 54
A novel mechanism of XIAP degradation induced by timosaponin AIII in hepatocellular carcinoma
Wang, N., Feng, Y., Zhu, M., Siu, F., Ng, K., & Che, C. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.07.018 · Cited by 52
Wang, G., Yu, Y., Tu, Y., Tong, J., Liu, Y., Zhang, C., Chang, Y., Wang, S., Jiang, C., Zhou, E., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0128292 · Cited by 52
Zhang, J., Zhu, S., Tan, Q., Cheng, D., Dai, Q., Yang, Z., Zhang, L., Li, F., Zuo, Y., Dai, W., et al. (2020) · Theranostics · doi:10.7150/thno.43932 · Cited by 52
“Autophagy is a conserved lysosome-based dynamic intracellular degradative process that plays an important role in regulating cellular homeostasis and responding to changes in nutrient status [1, 2].”
BackgroundShvets, E., & Elazar, Z. (2008) · Autophagy · doi:10.4161/auto.6823 · Cited by 43
Brinar, M., Vermeire, S., Cleynen, I., Lemmens, B., Sagaert, X., Henckaerts, L., Assche, G. V., Geboes, K. J., Rutgeerts, P. J., & Hertogh, G. D. (2011) · Journal of Crohn s and Colitis · doi:10.1016/j.crohns.2011.06.008 · Cited by 51
D’Antonio, M., Feltri, M. L., & Wrabetz, L. G. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22066 · Cited by 51
“Autophagy is defined as the process by which a portion of cytosol or organelle is sequestered in a double membrane structure called the autophagosome, which then fuses with lysosomes (Ohsumi, 2001).”
BackgroundThe Role of Macroautophagy in Development of Filamentous Fungi
Bartoszewska, M., & Kiel, J. A. K. W. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3528 · Cited by 52
“Phagophore formation involves two sets of proteins that each participate in two ubiquitin conjugation-like reactions (92).”
Castino, R., Davies, J., Beaucourt, S. M., Isidoro, C., & Murphy, D. (2005) · The FASEB Journal · doi:10.1096/fj.04-3162fje · Cited by 50
“While it is not difficult to imagine that autophagy, a process involving massive intracellular degradation, might promote neuronal death (31), this is contradicted by the similarly axiomatic concept that mammalian autophagy, as in yeast (32), is a prosurvival mechanism.”
BackgroundA truncating mutation in the autophagy gene UVRAG drives inflammation and tumorigenesis in mice
Quach, C., Song, Y., Guo, H., Li, S., Maazi, H., Fung, M., Sands, N. A., O’Connell, D., Restrepo-Vassalli, S., Chai, B., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13475-w · Cited by 54
Chang, C., Hseu, Y., Thiyagarajan, V., Lin, K., Way, T., Korivi, M., Liao, J., & Yang, H. (2017) · Archives of Toxicology · doi:10.1007/s00204-017-1967-0 · Cited by 52
The Function of Autophagy as a Regulator of Melanin Homeostasis
Lee, K. W., Kim, M.-J., Lee, S. H., & Kim, K. D. (2022) · Cells · doi:10.3390/cells11132085 · Cited by 53
Autophagy in CD4+ T-cell immunity and tolerance
Lünemann, J. D., & Münz, C. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.113 · Cited by 51
The involvement of cellular prion protein in the autophagy pathway in neuronal cells
Oh, J.-M., Shin, H., Park, S., Kim, B., Choi, J.-K., Choi, E., Carp, R. I., & Kim, Y. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.07.003 · Cited by 49
The Intriguing Life of Autophagosomes
Mijaljica, D., Prescott, M., & Devenish, R. J. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13033618 · Cited by 55
“Then, the E1 enzyme, Atg7 activates the processed LC3 and transfers it to Atg3 (functions like E2 enzyme).”
BackgroundInfluentialAtg9A Protein, an Autophagy-related Membrane Protein, Is Localized in the Neurons of Mouse Brains
Tamura, H., Shibata, M., Koike, M., Sasaki, M., & Uchiyama, Y. (2010) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.2010.955690 · Cited by 43
“These structures either receive lysosomal hydrolytic enzymes via transporting vesicles from the trans-Golgi network (TGN) or fuse with lysosomes to become autolysosomes (Klionsky and Emr 2000; Ohsumi 2001; Uchiyama et al. 2008).”
BackgroundLithium promotes recovery of neurological function after spinal cord injury by inducing autophagy
Zhang, D., Wang, F., Zhai, X., Li, X.-H., & He, X.-J. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.241473 · Cited by 49
“Although lithium has been widely used for safely and effectively treating neuropsychiatric disorders, it is rarely used for acute SCI (Ohsumi, 2001; Chang et al., 2011; Chen et al., 2013; Kim et al., 2013; Duo and He, 2015; Hou et al., 2015; Seo et al., 2015; Quartini et al., 2016; Zhou et al.,…”
BackgroundMethodThe role of FOXOs and autophagy in cancer and metastasis—Implications in therapeutic development
Farhan, M., Silva, M., Li, S., Yan, F., Fang, J., Peng, T., Hu, J., Tsao, M., Little, P. J., & Zheng, W. (2020) · Medicinal Research Reviews · doi:10.1002/med.21695 · Cited by 50
“Continued expansion of the autophagosomal membrane is regulated by the conjugation of essential autophagy genes Atg5 to Atg12 and of microtubule‐associated protein 1 light chain 3 alpha (LC3) to phosphatylethanolamine (PE), forming LC3‐PE conjugate (also known as LC3‐II).(119,123,126) The engulfment of the cytoplasmat…”
BackgroundInterplay between the Ubiquitin Proteasome System and Ubiquitin-Mediated Autophagy in Plants
Su, T., Yang, M., Wang, P., Zhao, Y., & Ma, C. (2020) · Cells · doi:10.3390/cells9102219 · Cited by 49
“This process starts with the cleavage of the ubiquitin-like protein ATG8 by the Cys protease ATG4 to expose a conserved C-terminal glycine, which is essential for the subsequent conjugation reaction [61,63].”
BackgroundAdenovirus Degradation of Cellular Proteins
Schreiner, S., Wimmer, P., & Dobner, T. (2012) · Future Microbiology · doi:10.2217/fmb.11.153 · Cited by 53
Davies, J., & Murphy, D. (2002) · Journal of Neuroendocrinology · doi:10.1046/j.1365-2826.2002.00822.x · Cited by 49
Kajstura, J., Bolli, R., Sonnenblick, E. H., Anversa, P., & Leri, A. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.12.013 · Cited by 49
Sasaki, M., Miyakoshi, M., Sato, Y., & Nakanuma, Y. (2011) · Digestive Diseases and Sciences · doi:10.1007/s10620-011-1929-y · Cited by 49
“Autophagy (hereafter referred to as autophagy) in human diseases has been highlighted during the last decade (12-14) and recent data demonstrated that autophagy is”
BackgroundInfluentialUbiquitin-like proteins and autophagy at a glance
Shpilka, T., Mizushima, N., & Elazar, Z. (2012) · Journal of Cell Science · doi:10.1242/jcs.093757 · Cited by 53
“This complex is essential for the formation and elongation of the autophagosome (Mizushima et al., 2001) and orthologs of this system, with the respective functionality, are found in yeast and mammals (Ohsumi, 2001).”
Background
Metadata
- Authors
- Ohsumi, Y.
- Affiliations
- National Institute for Basic Biology (JP)
- Corresponding author
- Ohsumi, Yoshinori
- ORCID
- Ohsumi, Yoshinori
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2001-03
- Volume
- 2
- Issue
- 3
- Pages
- 211-216
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2792139654
- Cited by
- 1,240
- References
- 45
- Citations by year
- 2026: 13 · 2025: 25 · 2024: 30 · 2023: 44 · 2022: 39 · 2021: 34 · 2020: 64 · 2019: 65 · 2018: 51 · 2017: 54 · 2016: 59 · 2015: 44 · 2014: 58 · 2013: 56 · 2012: 67
- FWCI
- 7.06
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › 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 › Cell Biology › Cellular transport and secretion
- Keywords
- autophagy, ubiquitin-like proteins, membrane dynamics, yeast, autophagy-related genes
- MeSH terms
- Autophagy-Related Protein 8 Family, Autophagy-Related Protein 7, Autophagy, Lysosomes, Microscopy, Electron, Microtubule-Associated Proteins, Models, Biological, Proteins, Saccharomyces cerevisiae, Ubiquitins, Vacuoles, Saccharomyces cerevisiae Proteins
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