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Atg8: an autophagy-related ubiquitin-like protein family.
Open accessAbstract
Autophagy-related (Atg) proteins are eukaryotic factors participating in various stages of the autophagic process. Thus far 34 Atgs have been identified in yeast, including the key autophagic protein Atg8. The Atg8 gene family encodes ubiquitin-like proteins that share a similar structure consisting of two amino-terminal α helices and a ubiquitin-like core. Atg8 family members are expressed in various tissues, where they participate in multiple cellular processes, such as intracellular membrane trafficking and autophagy. Their role in autophagy has been intensively studied. Atg8 proteins undergo a unique ubiquitin-like conjugation to phosphatidylethanolamine on the autophagic membrane, a process essential for autophagosome formation. Whereas yeast has a single Atg8 gene, many other eukaryotes contain multiple Atg8 orthologs. Atg8 genes of multicellular animals can be divided, by sequence similarities, into three subfamilies: microtubule-associated protein 1 light chain 3 (MAP1LC3 or LC3), γ-aminobutyric acid receptor-associated protein (GABARAP) and Golgi-associated ATPase enhancer of 16 kDa (GATE-16), which are present in sponges, cnidarians (such as sea anemones, corals and hydras) and bilateral animals. Although genes from all three subfamilies are found in vertebrates, some invertebrate lineages have lost the genes from one or two subfamilies. The amino terminus of Atg8 proteins varies between the subfamilies and has a regulatory role in their various functions. Here we discuss the evolution of Atg8 proteins and summarize the current view of their function in intracellular trafficking and autophagy from a structural perspective.
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“Yet in other settings, autophagy induction triggers a significant decrease in LC3-I levels, along with an increase in LC3-II levels, presumably due to its increased conversion into LC3-II [280].”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [280]
Experimental — accuracy not yet measuredIn the citing paper
“some studies suggest isoform specificity in selective autophagy (Shpilka et al., 2011; Maruyama et al., 2014; Koukourakis et al., 2015).”
From Microtubule-associated protein 1 light chain 3B, (LC3B) is necessary to maintain lipid-mediated homeostasis in the retinal pigment epithelium (2018) · cites this paper as Shpilka et al., 2011
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Cites
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LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
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“The motif in p62 responsible for binding Atg8, the LC3interacting region (LIR, also known as Atg8-interacting motif, AIM) [104,105], is common to other proteins that interact with Atg8 proteins, including Nbr1 [106], Atg3 [107], Nix [96] and the yeast cytoplasm-to-vacuole targeting receptor Atg19 [108].”
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“[113] show the conservation (overall height) and residue prevalence of multiple alignment positions.”
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“These adaptors bind simultaneously to Atg8 proteins and to ubiquitinated proteins, organelles, and in some cases pathogens [18,94,103].”
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“Sequences for the alignments were taken from the CDD [114] and PFAM [115] database entries cd01611 and PF02991, respectively, and sequences”
MethodA ubiquitin-like system mediates protein lipidation
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“Unlike ubiquitin, which is conjugated to a protein, Atg8 is covalently conjugated to PE lipid through its carboxy-terminal exposed glycine [64].”
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“Atg4 regulates a critical step in the autophagic process and is therefore subjected to regulation by reactive oxygen species, for example, which prevent it from reversing the conjugation of Atg8 proteins to PE during autophagy [83].”
BackgroundSelf-citation
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ACSL3 is a novel GABARAPL2 interactor that links ufmylation and lipid droplet biogenesis
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C/EBPβ-dependent autophagy inhibition hinders NK cell function in cancer
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“…main positive autophagy regulators,such as Irgm 55 , Mapk8 56 and Tp53 , genes that promote autophagy initiation, including Ulk1 , Ulk2 , Ambra , Becn1 , Prkaa1 , Pik3ra and Pik3c3 57 and members of the ATG8 58 and ATG12 ubiquitin-like conjugation system 59 , engaged in autophagosome bio-genesis.”
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“A commonly used marker is human microtubule-associated protein 1 A/1B-light chain 3 (MAP1LC3 or LC3), a member of the autophagy-related protein 8 (ATG8) family that is omnipresent in eukaryotes (Shpilka et al., 2011).”
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Dengjel, J., & Abeliovich, H. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2472-0 · Cited by 28
Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy
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“However, ATG8 proteins contain a supplementary hydrophobic pocket that engages interaction networks with autophagy and membrane trafficking components [57].”
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“ATG4C and ATG4A functions seem to be complementary and redundant to that of ATG4B [7], whereas ATG4D has been shown to prime and delipidate GABARAPL1 upon caspase-based activation in in vitro experiments [8].”
BackgroundInfluentialInhibition of autolysosome formation in host autophagy by Trypanosoma cruzi infection
Onizuka, Y., Takahashi, C., Uematsu, A., Shinjo, S., Seto, E., & Nakajima‐Shimada, J. (2017) · Acta Tropica · doi:10.1016/j.actatropica.2017.02.021 · Cited by 28
Selective binding of mitophagy receptor protein Bcl-rambo to LC3/GABARAP family proteins
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Facile synthesis of covalent probes to capture enzymatic intermediates during E1 enzyme catalysis
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Pan, J., Di, Y., Li, Y.-B., Chen, C., Wang, J., & Zhao, X. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004891 · Cited by 28
“The autophagy-related protein, microtubule-associated protein 1 light chain 3 (LC3, one isoform of ATG8) (33), was overexpressed as a fusion protein with the cell-penetrating TAT peptide and red fluorescent protein (RFP) (His-TAT-RFP-LC3-His) to detect autophagosomes in HaEpi (34).”
BackgroundSun, S., Wu, Y., Fu, H., Yang, M., Ge, X., Zhu, J. X., Xuan, F., & Wu, X. (2019) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2018.12.079 · Cited by 27
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“This allows the protein to become membrane-anchored to autophagosomes [25].”
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Unravelling the multifaceted roles of Atg proteins to improve cancer therapy
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“In mammals, Atg8 proteins fall under two subfamilies namely, microtubule-associated protein-1-light chain 3 (LC3), and Gammaaminobutyric acid receptor-associated protein (GABARAP)/Golgiassociated ATPase enhancer of 16 kDa (GATE-16) subfamilies (He et al., 2003; Shpilka et al., 2011; Weidberg et al., 2010; Xin et al.,…”
BackgroundStress - Regulation of SUMO conjugation and of other Ubiquitin‐Like Modifiers
Ilic, D., Magnussen, H., & Tirard, M. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.12.010 · Cited by 23
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Long, W., Zhang, L., Wang, Y., Xie, H., Wang, L., & Yu, H. (2022) · Journal of Oncology · doi:10.1155/2022/7032614 · Cited by 27
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“FYCO1 interacts with MAP1LC3/LC3 (microtubuleassociated protein 1 light chain 3, LC3 hereafter) proteins(31-33) that are lipidated to be anchored on both sides of the phagophoremembrane, where they act in recruitment of cargo and other autophagic proteins to phagophores, as well as in facilitation of phagophore expans…”
BackgroundSakurai, S., Tomita, T., Shimizu, T., & Ohto, U. (2017) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x17001911 · Cited by 25
Srinivasan, V., Bruelle, C., Scifo, E., Pham, D. D., Soliymani, R., Lalowski, M. M., & Lindholm, D. (2019) · iScience · doi:10.1016/j.isci.2019.100790 · Cited by 26
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“1).12 Both the ULK complex and WIPI2 are required for ATG9 trafficking to and possibly from the phagophore and omegasome.9 The growth of the phagophore, and its closure to become an autophagosome, requires the lipidated Atg8s, LC3 and GABARAPs.13 The Atg8’s are cytosolic proteins which become membrane associated by th…”
BackgroundIdentification of Atg8 Isoform in Encysting Acanthamoeba
Moon, E., Hong, Y., Chung, D.-I., & Kong, H.-H. (2013) · Korean Journal of Parasitology · doi:10.3347/kjp.2013.51.5.497 · Cited by 26
“Each Atg8 subfamily (GATE-16, GABARAP, and LC3) has a distinctive sequence feature [3].”
BackgroundInfluentialIndependent losses and duplications of autophagy‐related genes in fungal tree of life
Wang, Q., Liu, H., Xu, H., Hei, R., Zhang, S., Jiang, C., & Xu, J. (2018) · Environmental Microbiology · doi:10.1111/1462-2920.14451 · Cited by 26
Impairment of Proteasome and Autophagy Underlying the Pathogenesis of Leukodystrophy
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“The autophagy process is coordinately controlled by autophagy-related (ATG) proteins, among which microtubule-associated protein 1 light chain 3 (LC3), a mammalian Atg8 homolog, undergoes a unique ubiquitin-like conjugation to phosphatidylethanolamine on the autophagic membrane to formLC3-phosphatidylethanolamine conj…”
BackgroundAstaxanthin Inhibits Autophagic Cell Death Induced by Bisphenol A in Human Dermal Fibroblasts
Lim, S.-R., Kim, D. W., Sung, J., Kim, T., Choi, C., & Lee, S. (2021) · Antioxidants · doi:10.3390/antiox10081273 · Cited by 25
Autophagy: An Important Biological Process That Protects Plants from Stressful Environments
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“Among the ATG genes, ATG8 is the central protein involved in autophagy and also a marker for the autophgosome (Shpilka et al., 2011).”
BackgroundSancilio, S., Gallorini, M., Cataldi, A., Sancillo, L., Rana, R. A., & di Giacomo, V. (2017) · Journal of Periodontology · doi:10.1902/jop.2017.160629 · Cited by 25
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“Previous studies have shown that transcription of ATG8, a highly conserved gene required for phagophore formation during autophagy (Shpilka et al., 2011), is repressed in nutrient-rich conditions by the Rpd3–Sin3–Ume6 histone deacetylase (HDAC) complex (Bartholomew et al.”
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“There are six Atg8 family members in mammals, including LC3A, LC3B, LC3C, and GABARAP proteins [45] and two in Drosophila with Atg8a shown to be essential for autophagy [46].”
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Shrestha, B. K., Rasmussen, M. S., Abudu, Y. P., Bruun, J., Larsen, K. B., Alemu, E. A., Sjøttem, E., Lamark, T., & Johansen, T. (2020) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)49883-8 · Cited by 24
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“Out of the many ATG gene nucleotide sequences of eukaryotic organisms, from yeast to mammals [15,21,24], we were particularly interested in ATG1 and ATG8 because the ATG1 product plays an essential role in the regulation of autophagy [19,25], and the ATG8 product performs an important role in the formation of double-m…”
BackgroundThe two Dictyostelium discoideum autophagy 8 proteins have distinct autophagic functions
Meßling, S., Matthias, J., Xiong, Q., Fischer, S., & Eichinger, L. (2017) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2017.03.014 · Cited by 24
LC3A Silencing Hinders Aggresome Vimentin Cage Clearance in Primary Choroid Plexus Carcinoma
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“LC3 and GABARAP proteins are involved in various intracellular processes [10] and present specificities for cargo recognition [11,12].”
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“28,29 ATG8 is central to the yeast ALP 30,31 and six of its seven human homologs have also been shown to function in the ALP, but to our knowledge MAP1LC3B2 has not.”
BackgroundManipulation of selective macroautophagy by pathogens at a glance
Cong, Y., Dinesh Kumar, N., Mauthe, M., Verlhac, P., & Reggiori, F. (2020) · Journal of Cell Science · doi:10.1242/jcs.240440 · Cited by 23
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“83 Additionally, the mammalian ortholog of yeast ATG6, known as Beclin ‐ 1, plays a crucial role in autophagy.”
Molecular functions of autophagy adaptors upon ubiquitin-driven mitophagy
Yamano, K., & Kojima, W. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.129972 · Cited by 26
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“Core to the autophagic pathway is the ATG8 family of proteins (ATG8s) that, except for an N-terminal arm, structurally resemble the ubiquitin family of proteins (8).”
BackgroundHanley, S. E., Willis, S. D., & Cooper, K. F. (2021) · Autophagy · doi:10.1080/15548627.2021.1877934 · Cited by 22
Hu, P., Ren, Y., Xu, J., Luo, W., Wang, M., Song, P., Guan, Y., Hu, H., & Li, C. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.125526 · Cited by 22
Innate immune and proinflammatory signals activate the Hippo pathway via a Tak1-STRIPAK-Tao axis
Yang, Y., Zhou, H., Huang, X., Wu, C., Zheng, K., Deng, J., Zheng, Y., Wang, J., Chi, X., Ma, X., et al. (2024) · Nature Communications · doi:10.1038/s41467-023-44542-y · Cited by 22
“Atg8(LC3/GABARAPin mammals), a key autophagy-related protein in autophagosome formation, mediates the lysosomal degradation of cargo molecules by recruiting them into autophagosomes 46 .”
Qian, W., Lu, J., Gao, C., Liu, Q., Yao, W., Wang, T., Wang, X., & Wang, Z. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1336773 · Cited by 22
“Notably, Atg8 gene (Shpilka et al., 2011), encoding a core protein involved in autophagy, was signi fi cantly upregulated.”
BackgroundHuman GABARAP can restore autophagosome biogenesis in aC. elegans lgg-1mutant
Jenzer, C., Manil-Ségalen, M., Lefebvre, C., Largeau, C., Glatigny, A., & Legouis, R. (2014) · Autophagy · doi:10.4161/auto.29745 · Cited by 23
“Atg8 is highly conserved and presents numerous orthologs and paralogs in mammals, which have been classified as MAP1LC3/LC3 (microtubule-associated protein 1 light chain 3) and GABARAP (GABA[A] receptor-associated protein) subfamilies.(2) LC3 and GABARAP proteins act in diverse intracellular trafficking and autophagy…”
BackgroundWang, H., Pan, Y., Hu, P., Zhu, Y., Li, J., Jiang, X., & Liu, G. (2014) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2014.06.004 · Cited by 22
Matthias, J., Meßling, S., & Eichinger, L. (2015) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2015.10.007 · Cited by 22
Barthez, M., Poplineau, M., Elrefaey, M., Caruso, N., Graba, Y., & Saurin, A. J. (2020) · Scientific Reports · doi:10.1038/s41598-020-66377-z · Cited by 22
“…either ZKSCAN3 or ZKSCAN4 with M1BP RNAi and monitored autophagy induction by cytoplasmic Atg8a accumulation, which is a marker of early autophagy induction, where its nuclear export into the cytoplasm is followed by lipidation recruiting it to early autophagosome membranes (Shpilka et al., 2011).”
BackgroundLee, J., Yamaoka, Y., Kong, F., Cagnon, C., Beyly, A., Jang, S., Gao, P., Kang, B., Li‐Beisson, Y., & Lee, Y. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2005600117 · Cited by 22
“In addition to enzymes of lipid catabolism, CrATG8, a Chlamydomonas ortholog of ATG8, a critical factor of autophagy in a wide range of organisms (39), was also reported to be necessary for lipid remobilization in Chlamydomonas (40), suggesting a role of autophagy in the process.”
BackgroundQuantitative Models of Lipid Transfer and Membrane Contact Formation
Zhang, Y., Ge, J., Bian, X., & Kumar, A. (2022) · Contact · doi:10.1177/25152564221096024 · Cited by 23
“We hypothesize that the concentration of lipidated ATG8 contributes most to the osmotic membrane tension of phagophores, which in turn regulates lipid flow to phagophore by ATG2, in addition to the many other functions of ATG8 lipidation in autophagy (Shpilka et al., 2011).”
BackgroundMitophagy Induced by Metal Nanoparticles for Cancer Treatment
Mundekkad, D., & Cho, W. C. S. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14112275 · Cited by 21
Friends and Foes: The Ambivalent Role of Autophagy in HIV-1 Infection
Klute, S., & Sparrer, K. M. J. (2024) · Viruses · doi:10.3390/v16040500 · Cited by 21
“…E1-like enzyme, ATG3 acts as Here, ATG7 serves as an E1-like enzyme, ATG3 acts as the E2-like enzyme and the ATG5–ATG12–ATG16L1 complex represents the E3-ligase-like protein ligase [15,16]. the E2-like enzyme and the ATG5–ATG12– ATG16L1 complex represents the E3-ligase-like protein ligase [15,16].”
The Function of Autophagy in Lace Plant Programmed Cell Death
Dauphinee, A. N., Denbigh, G. L., Rollini, A., Fraser, M. S., Lacroix, C. R., & Gunawardena, A. H. L. A. N. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.01198 · Cited by 21
Zhang, H., Li, Y., Lai, W., Huang, K. L., Li, Y., Wang, Z., Chen, X., & Wang, A. (2021) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2021.103632 · Cited by 20
The Role of WIPI2, ATG16L1 and ATG12-ATG5 in Selective and Nonselective Autophagy
Campisi, D., Hawkins, N., Bonjour, K., & Wollert, T. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169138 · Cited by 22
LGG-1/GABARAP lipidation is not required for autophagy and development in Caenorhabditis elegans
Leboutet, R., Largeau, C., Müller, L., Prigent, M., Quinet, G., Rodríguez, M. S., Cuif, M., Hoppe, T., Culetto, E., Lefebvre, C., et al. (2023) · eLife · doi:10.7554/elife.85748 · Cited by 20
“There are seven isoforms of Atg8 homologs in 52 humans defining two families, the MAP-LC3 (abbreviated as LC3A-a, LC3A-b, LC3B, LC3C) and 53 the GABARAP (GABARAP, GABARAPL1, GABARAPL2) (Shpilka et al., 2011).”
In vitro systems for Atg8 lipidation
Zens, B., Sawa-Makarska, J. Z., & Martens, S. (2014) · Methods · doi:10.1016/j.ymeth.2014.11.004 · Cited by 20
Essential Role for the Mammalian ATG8 Isoform LC3C in Xenophagy
Shpilka, T., & Elazar, Z. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.10.020 · Cited by 21
“Yeasts possess one ATG8 gene, whereas humans have six ATG8 genes that can be grouped into three subfamilies: GATE16, GABARAP (including GABARPAP and GABARAPl1), and LC3 (including LC3A, LC3B, and LC3C) (Shpilka et al., 2011).”
BackgroundScaffold proteins in bulk and selective autophagy
Eickhorst, C., Licheva, M., & Kraft, C. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.01.009 · Cited by 22
Choi, J., Biering, S. B., & Hwang, S. (2016) · Small GTPases · doi:10.1080/21541248.2016.1213090 · Cited by 22
“Multiple LC3 homologs exist in mammalian systems, and they act in different stages of autophagosome formation.(30) The LC3 subfamily (LC3A and LC3B inmice) functions in elongation”
BackgroundNeves, J., Sampaio, M., Séneca, A., Pereira, S., Pissarra, J., & Pereira, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910644 · Cited by 19
Size, organization, and dynamics of soluble SQSTM1 and LC3-SQSTM1 complexes in living cells
Kraft, L. J., Dowler, J., Manral, P., & Kenworthy, A. K. (2016) · Autophagy · doi:10.1080/15548627.2016.1199299 · Cited by 23
“Since LC3 itself is structurally similar to ubiquitin, it has been dubbed a ubiquitin-like protein.(7) Interestingly, LC3 associates with slowly diffusing, high molecular weight complexes in both the cytoplasm and nucleus.”
BackgroundCarbofuran accelerates the cellular senescence and declines the life span of spns1 mutant zebrafish
Khan, A., Fahad, T. M., Akther, T., Zaman, T., Hasan, M. F., Khan, M. R. I., Islam, M. S., & Kishi, S. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16171 · Cited by 19
Autophagy participates in the unfolded protein response in Toxoplasma gondii
Nguyen, H. M., Berry, L., Sullivan, W. J., & Besteiro, S. (2017) · FEMS Microbiology Letters · doi:10.1093/femsle/fnx153 · Cited by 20
Lysosome-associated CASM: from upstream triggers to downstream effector mechanisms
Kaur, N., Carlsson, S. R., & Lystad, A. H. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1559125 · Cited by 19
Abert, C., Kontaxis, G., & Martens, S. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.736892 · Cited by 18
“Although there is only one Atg8 protein in Saccharomyces cerevisiae, higher eukaryotes have several ATG8 proteins (subdivided in the LC3 and the GABARAP groups) (7).”
The Multi-Faceted Role of Autophagy During Animal Virus Infection
Jiang, H., Kan, X., Ding, C., & Sun, Y. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.858953 · Cited by 19
“This process requires two ubiquitin-like conjugation systems: the ATG12-ATG5-ATG16L1 system and the LC3 system (Mizushima et al., 2011; Shpilka et al., 2011).”
BackgroundUmesh, Prerna, K., & Dubey, V. K. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1869100 · Cited by 17
A RabGAP negatively regulates plant autophagy and immune trafficking
Yuen, E. L. H., Leary, A. Y., Clavel, M., Tümtaş, Y., Mohseni, A., Zhao, J., Picchianti, L., Jamshidiha, M., Pandey, P., Duggan, C., et al. (2024) · Current Biology · doi:10.1016/j.cub.2024.04.002 · Cited by 17
Liu, Q., Zhou, D.-X., Sun, L., Luo, L., Wu, C., Lin, P., & Han, S. (2014) · Pathology Research International · doi:10.1155/2014/104962 · Cited by 17
“Thus far 34 autophagy-related genes (Atg) have been identified in yeast [17].”
Dictyostelium discoideum and autophagy – a perfect pair
Fischer, S., & Eichinger, L. (2019) · The International Journal of Developmental Biology · doi:10.1387/ijdb.190186le · Cited by 19
“Three are grouped into the MAP1-LC3 (microtubule-associated protein 1 – light chain 3) and four into the GABARAP/GATE16 (Gamma-aminobutyric acid receptor-associated protein/Golgi-associated ATPase enhancer of 16 kDa) subfamily (Shpilka et al., 2011).”
BackgroundLi, X., Li, Z., Zhu, H., & Yu, X. (2020) · BioMed Research International · doi:10.1155/2020/8537381 · Cited by 19
“In order to provide a comparison, we constructed risk signatures based on LC3-coding genes [26, 27].”
MethodSmall but mighty: Atg8s and Rabs in membrane dynamics during autophagy
Barz, S., Kriegenburg, F., Sánchez‐Martín, P., & Kraft, C. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119064 · Cited by 17
Autophagy modulates cell fate decisions during lineage commitment
Sharma, K., Asp, N., Harrison, S. P., Siller, R., Baumgarten, S., Gupta, S., Chollet, M. E., Andersen, E. W., Sullivan, G. J., & Simonsen, A. (2021) · Autophagy · doi:10.1080/15548627.2021.2008691 · Cited by 16
“The ATG12– ATG5-ATG16L1 complex further facilitates the conjugation of Atg8 homolog proteins of the MAP1LC3/LC3 (microtubule associated protein 1 light chain 3) and GABARAP (GABA type A receptor-associated protein) subfamilies to phosphatidylethanolamine (PE) in the autophagic membrane to allow cargo selection and aut…”
BackgroundInteraction of ToLCNDV TrAP with SlATG8f marks it susceptible to degradation by autophagy
Prasad, A., & Prasad, M. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04281-7 · Cited by 17
“ATG8 is involved in recruiting cargo to autophagosomes which in turn deliver the cargo to vacuoles for their degradation [19].”
BackgroundNdolo, R. O., Yu, L., Zhao, Y. M., Lu, J., Wang, G., Xinmin, Z., Ren, Y., & Yang, J. (2023) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000530605 · Cited by 16
Klińska, S., Kędzierska, S., Demski, K., & Banaś, A. (2023) · BMC Plant Biology · doi:10.1186/s12870-023-04379-5 · Cited by 16
“Atg8 present at the outer membrane of autophagosome is not degraded and can be recycled [25, 44, 47].”
BackgroundUbiquitination of CD47 Regulates Innate Anti‐Tumor Immune Response
Gou, Q., Yan, B., Duan, Y., Guo, Y., Qian, J., Shi, J., & Hou, Y. (2024) · Advanced Science · doi:10.1002/advs.202412205 · Cited by 19
Anesthesia with Disuse Leads to Autophagy Up-regulation in the Skeletal Muscle
Kashiwagi, A., Hosokawa, S., Maeyama, Y., Ueki, R., Kaneki, M., Martyn, J. A. J., & Yasuhara, S. (2014) · Anesthesiology · doi:10.1097/aln.0000000000000561 · Cited by 16
Antiproliferative effects of L‑asparaginase in acute myeloid leukemia
Chen, T., Zhang, J., Zeng, H., Zhang, Y., Zhang, Y., Zhou, X., & Zhou, H. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.8904 · Cited by 18
“I is modified by shearing and ubiquitination, before being coupled with phosphatidylethanolamine on the surface of the autophagosome membrane to form a membrane-bound LC3-II, located on the inner and outer membranes of the autophagosome (24,26).”
BackgroundInfluentialUnlocking the gate to GABARAPL2
Chan, J. C. Y., & Gorski, S. M. (2022) · Biologia Futura · doi:10.1007/s42977-022-00119-2 · Cited by 16
Taniguchi, S., Toyoshima, M., Takamatsu, T., & Mima, J. (2020) · Protein Science · doi:10.1002/pro.3828 · Cited by 16
Mitophagy in fibrotic diseases: molecular mechanisms and therapeutic applications
Cui, X. T., Zhou, Z., Tu, H., Wu, J., Zhou, J. P., Yi, Q., Liu, O., & Dai, X. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1430230 · Cited by 17
Radiation Hormesis to Improve the Quality of Adult Spodoptera litura (Fabr.)
Vimal, N., Angmo, N., Sengupta, M., & Seth, R. K. (2022) · Insects · doi:10.3390/insects13100933 · Cited by 15
“Some reports also have showed increased atg8 gene levels under stress conditions, and Foxo1, Foxo3, and E2F1 may help in the transcriptional regulation of atg8 [66].”
Background
Metadata
- Authors
- Shpilka, T., Weidberg, H., Pietrokovski, S., & Elazar, Z.
- Affiliations
- Weizmann Institute of Science (IL)
- Corresponding author
- Pietrokovski, Shmuel
- Elazar, Zvulun
- Venue
- Genome biology
- Published
- 2011
- Volume
- 12
- Issue
- 7
- Pages
- 226
- ISSN
- 1465-6906 (ISSN-L)
- PMC
- PMC3218822
- OpenAlex
- W2034198209
- Cited by
- 543
- References
- 115
- Citations by year
- 2026: 25 · 2025: 41 · 2024: 38 · 2023: 37 · 2022: 34 · 2021: 56 · 2020: 45 · 2019: 39 · 2018: 31 · 2017: 39 · 2016: 49 · 2015: 29 · 2014: 36 · 2013: 25 · 2012: 19
- FWCI
- 3.00
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Genome biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Eli Lilly and Company
- Legacy Heritage Fund
- Hermann und Lilly Schilling-Stiftung für Medizinische Forschung
- 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
- ATG8, autophagy-related proteins, ubiquitin-like proteins, autophagy, autophagosome formation, phosphatidylethanolamine conjugation, LC3, GABARAP, protein evolution, intracellular membrane trafficking
- MeSH terms
- Animals, Autophagy, Humans, Ubiquitins, Evolution, Molecular, Protein Transport
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