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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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Items 201–300 of 1,001
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“To tackle these questions, we decided to use baker’s yeast (Saccharomyces cerevisiae) as a model system, since (i) it constitutes a well-established (chronological) aging model [16]; (ii) autophagy was discovered and largely uncovered in this model [17–19]; and (iii) MetR can be reliably controlled by virtue of media…”
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BackgroundHistone deacetylase inhibitors and cell death
Zhang, J., & Zhong, Q. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1656-6 · Cited by 229
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Gorski, S. M., Chittaranjan, S., Pleasance, E. D., Freeman, J. D., Anderson, C. L., Varhol, R. J., Coughlin, S. M., Zuyderduyn, S. D., Jones, S. J. M., & Marra, M. A. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00082-4 · Cited by 213
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Mariño, G., Urı́a, J. A., Puente, X. S., Quesada, V., Bordallo, J., & López-Otı́n, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208247200 · Cited by 206
RetractedAutophagy: An Intracellular Degradation Pathway Regulating Plant Survival and Stress Response
Su, T., Li, X., Yang, M., Shao, Q., Zhao, Y., Ma, C., & Wang, P. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.00164 · Cited by 211
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BackgroundTassa, A., Roux, M.-P., Attaix, D., & Béchet, D. (2003) · Biochemical Journal · doi:10.1042/bj20030826 · Cited by 210
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Mayran, N., Parton, R. G., & Gruenberg, J. E. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg321 · Cited by 207
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Sou, Y., Tanida, I., Komatsu, M., Ueno, T., & Kominami, E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505888200 · Cited by 214
Ko, A., Kanehisa, A., Martins, I., Senovilla, L., Chargari, C., Dugué, D., Mariño, G., Kepp, O., Michaud, M., Perfettini, J., et al. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.124 · Cited by 212
“is based on subsequent protein conjugation steps.(10) The initial formation of ATG5–ATG12 complexes allows for the recruitment of ATG8 (LC3 in mammalian cells) by phospha-”
BackgroundStarving Neurons Show Sex Difference in Autophagy
Du, L., Hickey, R. W., Bayir, H., Watkins, S. C., Tyurin, V. A., Guo, F., Kochanek, P. M., Jenkins, L. W., Ren, J., Gibson, G., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m804396200 · Cited by 204
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Vierstra, R. D. (2012) · PLANT PHYSIOLOGY · doi:10.1104/pp.112.200667 · Cited by 208
“In a unique twist, ATG8 is attached instead to the amine group of the lipid phosphatidylethanolamine (PE) and becomes membrane bound (Ohsumi, 2001; Klionsky, 2007).”
BackgroundInterplay Between Lipid Metabolism and Autophagy
Xie, Y., Li, J., Kang, R., & Tang, D. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00431 · Cited by 205
“Subsequent to nucleation, the phagophore expands by membrane addition, which is accomplished by 2 ubiquitin-like (Ubl) conjugation systems, the ATG12-ATG5 conjugation system and the microtubule-associated protein 1 light chain 3 (MAP1LC3/LC3) conjugation system (Ohsumi, 2001).”
BackgroundTolkovsky, A. M., Xue, L., Fletcher, G. C., & Borutaite, V. (2002) · Biochimie · doi:10.1016/s0300-9084(02)01371-8 · Cited by 206
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Massey, A. C., Kiffin, R., & Cuervo, A. M. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.04.010 · Cited by 202
Host immune responses to Toxoplasma gondii
Sasai, M., Pradipta, A., & Yamamoto, M. (2018) · International Immunology · doi:10.1093/intimm/dxy004 · Cited by 202
Endocytosis and Autophagy: Exploitation or Cooperation?
Tooze, S. A., Abada, A., & Elazar, Z. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018358 · Cited by 202
“In the first system, Atg7 and Atg10, E1-like-activating, and E2-like-conjugating enzyme, respectively, conjugate the ubiquitin-like molecule Atg12 to Atg5 (Ohsumi 2001).”
BackgroundChung, T., Suttangkakul, A., & Vierstra, R. D. (2009) · Plant Physiology · doi:10.1104/pp.108.126714 · Cited by 221
“The conjugation cascades center around two Ub-fold proteins, ATG8 and ATG12, which become covalently attached to their respective targets, the lipid phosphatidylethanolamine (PE) and the ATG5 protein, by a process mechanistically similar to ubiquitination (Ohsumi, 2001).”
BackgroundInfluentialAutophagy: Regulation and role in disease
Meijer, A. J., & Codogno, P. (2009) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360903044068 · Cited by 215
“Both Atg5Atg12 and Atg8-PE are produced by two unique, ubiquitin-like conjugation systems: the formation of Atg5-Atg12 requires Atg7 (homologous to the E1 ubiquitin-activating enzyme) and Atg10 (homologous to the E2 ubiquitin-activating enzyme), whereas conjugation of PE with Atg8 (a ubiquitin-like protein) requires A…”
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Takeuchi, S., Zhang, W., Wakamatsu, K., Ito, S., Hearing, V. J., Kraemer, K. H., & Brash, D. E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403994101 · Cited by 196
Medina, D. X., Caccamo, A., & Oddo, S. (2010) · Brain Pathology · doi:10.1111/j.1750-3639.2010.00430.x · Cited by 200
“The latter is commonly used to measure the levels of autophagy induction as it is derived from LC3-I during autophagy induction and incorporated into the growing membrane of autophagosomes (24).”
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Autophagy in Yeast: A Review of the Molecular Machinery.
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Pichler, A., & Melchior, F. (2002) · Traffic · doi:10.1034/j.1600-0854.2002.30601.x · Cited by 194
Wang, S., & Blumwald, E. (2014) · The Plant Cell · doi:10.1105/tpc.114.133116 · Cited by 193
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Yoshioka (1992) · International Journal of Oncology · doi:10.3892/ijo_00000028 · Cited by 192
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Role of Unc51.1 and its binding partners in CNS axon outgrowthPreprint
Tomoda, T., Kim, J. H., Zhan, C., & Hatten, M. E. (2004) · Genes & Development · doi:10.1101/gad.1151204 · Cited by 194
Chen, R., Zou, Y., Mao, D., Sun, D., Gao, G., Shi, J., Liu, X., Zhu, C., Yang, M., Ye, W., et al. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201403009 · Cited by 191
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Gómez-Santos, C., Ferrer, I., Santidrián, A. F., Barrachina, M., Gil, J., & Ambrosio, S. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10663 · Cited by 188
Asanuma, K., Tanida, I., Shirato, I., Ueno, T., Takahara, H., Nishitani, T., Kominami, E., & Tomino, Y. (2003) · The FASEB Journal · doi:10.1096/fj.02-0580fje · Cited by 186
Yang, M., Zhang, Y., Xie, X., Yue, N., Li, J., Wang, X., Han, C., Yu, J., Liu, Y., & Li, D. (2018) · The Plant Cell · doi:10.1105/tpc.18.00122 · Cited by 186
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BackgroundOhshima, T., Koga, H., & Shimotohno, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403866200 · Cited by 187
The ubiquitin‐proteasome pathway
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Izumi, M., Wada, S., Makino, A., & Ishida, H. (2010) · PLANT PHYSIOLOGY · doi:10.1104/pp.110.158519 · Cited by 182
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Gutierrez, M. G., Saka, H. A., Chinen, I., Zoppino, F. C. M., Yoshimori, T., Bocco, J. L., & Colombo, M. I. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601437104 · Cited by 174
Rajendran, R., Garva, R., Krstic–Demonacos, M., & Demonacos, C. (2011) · BioMed Research International · doi:10.1155/2011/368276 · Cited by 180
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Panyasrivanit, M., Khakpoor, A., Wikan, N., & Smith, D. R. (2009) · Journal of General Virology · doi:10.1099/vir.0.005355-0 · Cited by 178
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Sugawara, K., Suzuki, N. N., Fujioka, Y., Mizushima, N., Ohsumi, Y., & Inagaki, F. (2004) · Genes to Cells · doi:10.1111/j.1356-9597.2004.00750.x · Cited by 158
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Parekh, V. V., Wu, L., Boyd, K. L., Williams, J. A., Gaddy, J. A., Olivares–Villagómez, D., Cover, T. L., Zong, W., Zhang, J., & Kaer, L. V. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202071 · Cited by 166
Raben, N., Schreiner, C. N., Baum, R., Takikita, S., Xu, S., Xie, T., Myerowitz, R., Komatsu, M., van der Meulen, J. H., Nagaraju, K., et al. (2010) · Autophagy · doi:10.4161/auto.6.8.13378 · Cited by 168
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“Subsequently, the phagophore expands by membrane addition though two ubiquitin-like modification processes, among which ATG12-conjugation and microtubule-associated protein 1A/1B-light chain 3 (LC3)modification play the most crucial roles (Ohsumi, 2001; Tanida et al., 2004).”
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Crespo, J. L., Díaz‐Troya, S., & Florencio, F. J. (2005) · PLANT PHYSIOLOGY · doi:10.1104/pp.105.070847 · Cited by 161
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Neuronal macroautophagy: From development to degeneration
Boland, B., & Nixon, R. A. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.009 · Cited by 163
New Insights into the Mechanisms of Macroautophagy in Mammalian Cells
Eskelinen, E. (2008) · International review of cytology · doi:10.1016/s1937-6448(07)66005-5 · Cited by 161
Autophagy—A double‐edged sword in oncology
Apel, A., Zentgraf, H., Büchler, M. W., & Herr, I. (2009) · International Journal of Cancer · doi:10.1002/ijc.24500 · Cited by 162
Redox Control of the Survival of Healthy and Diseased Cells
Zhang, Y., Du, Y., Le, W., Wang, K., Kieffer, N., & Zhang, J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3685 · Cited by 161
“ROS target on the conserved residue Cys 81 of Atg4s, which is in the vicinity of the catalytic Cys 77 residue; oxidation of cysteines inhibits Atg4s protease activity and promotes lipidation of Atg8/LC3, an essential step for autophagy (17, 116, 130, 268).”
InfluentialSUMO: of branched proteins and nuclear bodies
Seeler, J.-S., & Dejean, A. (2001) · Oncogene · doi:10.1038/sj.onc.1204758 · Cited by 153
Autophagy in the heart and liver during normal aging and calorie restriction
Wohlgemuth, S. E., Julian, D., Akin, D. E., Fried, J., Toscano, K., Leeuwenburgh, C., & Dunn, Jr. (2007) · Rejuvenation Research · doi:10.1089/rej.2006.0535 · Cited by 179
“The E1-enzyme Atg 7 is essential for the formation of LC3-II (the membrane-bound form), thereby determining its tissue level 60 .”
Yamada, Y., Suzuki, N. N., Hanada, T., Ichimura, Y., Kumeta, H., Fujioka, Y., Ohsumi, Y., & Inagaki, F. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611473200 · Cited by 152
Self-citationQi, H., Xia, F., Xie, L., Yu, L., Chen, Q., Zhuang, X., Wang, Q., Li, F., Jiang, L., Xie, Q., et al. (2017) · The Plant Cell · doi:10.1105/tpc.17.00056 · Cited by 149
“Finally, two ubiquitin-like conjugation pathways, ATG8-PE and ATG12-ATG5, function in mature autophagosomeformationandcargoengulfment (Ohsumi,2001;Geng and Klionsky, 2008; Liu and Bassham, 2012; Li and Vierstra, 2012).”
BackgroundDisruption of Neuronal Autophagy by Infected Microglia Results in Neurodegeneration
Alirezaei, M., Kiosses, W. B., Flynn, C. T., Brady, N. R., & Fox, H. S. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002906 · Cited by 151
“To date, several autophagy related genes (Atg) and their respective proteins are known to directly regulate the formation of AV in mammalian cells [2,6].”
BackgroundInvolvement of ROS in Curcumin-induced Autophagic Cell Death
Lee, Y. J., Kim, N., Suh, Y., & Lee, C. (2011) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2011.15.1.1 · Cited by 148
New advances in autophagy in plants: Regulation, selectivity and function
Wang, P., Mugume, Y., & Bassham, D. C. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.07.018 · Cited by 150
“From analysis based primarily on yeast (Saccharomyces cerevisiae), 36 ATG proteins that drive the autophagic process have been described [10].”
Redox Control of Protein Kinase C: Cell- and Disease-Specific Aspects
Giorgi, C., Agnoletto, C., Baldini, C., Bononi, A., Bonora, M., Marchi, S., Missiroli, S., Patergnani, S., Poletti, F., Rimessi, A., et al. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2825 · Cited by 152
“The ubiquitin–proteasome and autophagy–lysosomal pathways are the two major routes for protein and organelle clearance in eukaryotic cells (189).”
Li, Y., Zhang, F., Zeng, C., Luo, W., Xiao, W., Gao, S., & Lei, G. (2015) · Joint Bone Spine · doi:10.1016/j.jbspin.2015.06.009 · Cited by 146
Dengjel, J., Høyer-Hansen, M. H., Nielsen, M. O., Eisenberg, T., Harder, L. M., Schandorff, S., Farkas, T., Kirkegaard, T., Becker, A. C., Schroeder, S., et al. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.014035 · Cited by 148
“The process is controlled by a set of evolutionarily conserved autophagy-related proteins (Atg proteins) initially identified in yeast (11, 12).”
BackgroundCK1α suppresses lung tumour growth by stabilizing PTEN and inducing autophagy
Cai, J., Li, R., Xu, X., Zhang, L., Lian, R., Fang, L., Huang, Y., Feng, X., Liu, X., Xu, L., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0065-8 · Cited by 146
Deng, S., Zhou, H., Xiong, R., Lu, Y., Yan, D., Xing, T., Dong, L., Tang, E., & Yang, H. (2006) · Breast Cancer Research and Treatment · doi:10.1007/s10549-006-9393-7 · Cited by 145
“The function of SMT3A in ubiquitin–proteasome system is similar to ubiquitin, and conjunction of SMT3A to its substrate also proceeds through this three-step cascade [39].”
BackgroundAsakura, M., Ninomiya, S., Sugimoto, M., Oku, M., Yamashita, S., Okuno, T., Sakai, Y., & Takano, Y. (2009) · The Plant Cell · doi:10.1105/tpc.108.060996 · Cited by 145
“Atg8 localizes at the autophagosomal membranes during the autophagic process; therefore, GFP-Atg8 can be used as a general marker for autophagy (Klionsky and Ohsumi, 1999; Ohsumi, 2001).”
BackgroundObara, K., Noda, T., Niimi, K., & Ohsumi, Y. (2008) · Genes to Cells · doi:10.1111/j.1365-2443.2008.01188.x · Cited by 150
“Conjugation of two ubiquitin-like molecules is essential for autophagy (Ohsumi, 2001): Atg12 is covalently conjugated to Atg5, and Atg8 is conjugated PE (Mizushima et al .”
BackgroundSelf-citationThe cell biology of autophagy in metazoans: a developing story
Meléndez, A., & Neufeld, T. P. (2008) · Development · doi:10.1242/dev.016105 · Cited by 145
Fujioka, Y., Noda, N. N., Nakatogawa, H., Ohsumi, Y., & Inagaki, F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.053520 · Cited by 143
Self-citationAutophagy in animal development
Allen, E. A., & Baehrecke, E. H. (2020) · Cell Death & Differentiation · doi:10.1038/s41418-020-0497-0 · Cited by 127
Schink, K. O., Raiborg, C., & Stenmark, H. (2013) · BioEssays · doi:10.1002/bies.201300064 · Cited by 150
“Isolation of autophagy (Atg) mutants of budding yeast has led to a molecular dissection of the autophagic machinery [79], and these studies revealed that the class III PI 3-kinase subunits Vps34, Vps15 and Vps30/Atg6 (homologue of mammalian Beclin 1) are essential for starvation-induced autophagy in yeast.”
BackgroundLong non-coding RNAs involved in autophagy regulation
Yang, L., Wang, H., Shen, Q., Feng, L., & Jin, H. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.464 · Cited by 142
Oxidative stress-induced apoptosis and autophagy: Balancing the contrary forces in spermatogenesis
Sharma, P., Kaushal, N., Saleth, L. R., Ghavami, S., Dhingra, S., & Kaur, P. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166742 · Cited by 148
Cotán, D., Cordero, M. D., Garrido‐Maraver, J., Oropesa-Ávila, M., Rodríguez‐Hernández, Á., Izquierdo, L. G., de la Mata, M., de Miguel, M., Lorite, J. B., Rivas, E., et al. (2011) · The FASEB Journal · doi:10.1096/fj.10-165340 · Cited by 142
“The molecular mechanism underlying autophagy has been extensively researched in the past decade, and the genes participating in this process, denoted ATGs (41), were found to be conserved from yeast to humans (42, 43).”
BackgroundAutophagy in plants: Physiological roles and post‐translational regulation
Qi, H., Xia, F., & Xiao, S. (2020) · Journal of Integrative Plant Biology · doi:10.1111/jipb.12941 · Cited by 144
“Ubiquitin‐like conjugation during plant autophagy In yeast, two ubiquitin‐like conjugation systems that decorate the phagophore with the Ub‐fold protein ATG8 are essential for vesicle formation (Ohsumi 2001; Yang and Klionsky, 2009).”
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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