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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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MethodA ubiquitin-like system mediates protein lipidation
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BackgroundSelf-citation
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Items 301–400 of 544
Molecular structures and function of the autophagosome-lysosome fusion machinery
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Ma, P., Schillinger, O., Schwarten, M., Lecher, J., Hartmann, R., Stoldt, M., Mohrlüder, J., Olubiyi, O. O., Strodel, B., Willbold, D., et al. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00366 · Cited by 15
Deficiency of GABARAP but Not Its Paralogs Causes Enhanced EGF-Induced EGFR Degradation
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“All sequences with this invariant feature form a strongly supported clade in our tree with the same relative position as the GABARAPL2/GATE16 clade presented by Shpilka et al.(19) Conversely, their GABARAP clade occupies the same position as our GABARAPL2 clade (their Fig.”
BackgroundInfluentialHuman ubiquitin-like proteins as central coordinators in autophagy
Mohan, J., & Wollert, T. (2018) · Interface Focus · doi:10.1098/rsfs.2018.0025 · Cited by 15
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Visual feedback neurons fine-tune Drosophila male courtship via GABA-mediated inhibition
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Zhao, J., Li, Z., & Li, J. (2021) · FEBS Open Bio · doi:10.1002/2211-5463.13340 · Cited by 12
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“ATG8 orthologs in higher eukaryotes are known to act at different steps of autophagy [34], however the role of ATG8s and autophagy pathway in sugarcane response to SrMV attack needs to be further investigated.”
BackgroundThe LC3B FRET biosensor monitors the modes of action of ATG4B during autophagy in living cells
Gökerküçük, E. B., Cheron, A., Tramier, M., & Bertolin, G. (2023) · Autophagy · doi:10.1080/15548627.2023.2179845 · Cited by 12
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“The Atg8 protein family which encodes ubiquitin-like proteins participate in various stages of the important autophagic process like intracellular membrane trafficking.(49) Only recently it was reported that a trafficking pathway of anthocyanins, co-localized in an endomembrane system, overlaps with the endoplasmic re…”
BackgroundFerreira, J. C. C., Lopes, C., Preto, A., Gonçalves, M. S. T., & Sousa, M. J. (2021) · Journal of Fungi · doi:10.3390/jof7110971 · Cited by 11
“During the course of autophagy, Atg8p is incorporated into the autophagosome and carried to the vacuolar lumen where it is degraded by the vacuolar hydrolases [51,52]; the hydrolysis of GFP-ATG8 results in free GFP that can be detected as an autophagy indicator.”
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Mechanisms and roles of membrane-anchored ATG8s
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“Notably, as shown in Motif I, a conserved glycine was identified at the C-terminal of the protein, which is typical of the ATG8 family [28] (Figure 1D).”
Selective autophagy goes exclusive
Johansen, T., & Lamark, T. (2014) · Nature Cell Biology · doi:10.1038/ncb2961 · Cited by 12
Mechanistically Dissecting Autophagy: Insights from In Vitro Reconstitution
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“The core regulatory modules include a serine/threonine kinase complex (mammals: ULK1/ULK2, FIP200/RB1CC1, ATG13, and ATG101; yeast: Atg1, Atg17, Atg13, plus Atg29 and Atg31 in Saccharomyces cerevisiae or Atg101 in Schizosaccharomyces pombe) (18–21), a class III phosphatidylinositol-3 kinase (PI3K) complex (mammals: AT…”
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Li, J., Zhang, L., Xia, Q., Fu, J., Zhou, Z., & Lin, F. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.08.164 · Cited by 12
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BackgroundInfluentialContribution of Autophagy to Cellular Iron Homeostasis and Stress Adaptation in Alternaria alternata
Wu, P., Choo, Y.-L., Wei, S.-Y., Yago, J. I., & Chung, K.-R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25021123 · Cited by 11
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BackgroundThe multiple roles of autophagy in uveal melanoma and the microenvironment
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“This complex is localized on the outer membrane surface of the preau-tophagosomal structure and is involved in expansion of the preautophagosomal outer membrane (Mizushima et al. 2011; Shpilka et al. 2011; Tsuboyama et al. 2016).”
BackgroundAutophagy and Respiratory Viruses: Mechanisms, Viral Exploitation, and Therapeutic Insights
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Aedes albopictus Autophagy-Related Gene 8 (AaAtg8) Is Required to Confer Anti-Bacterial Gut Immunity
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Jasieniecka‐Gazarkiewicz, K., Demski, K., Gidda, S. K., Klińska, S., Niedojadło, J., Lager, I., Carlsson, A. S., Minina, E. A., Mullen, R. T., Bozhkov, P. V., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063006 · Cited by 11
“During various stress conditions, up-regulation of ATG8 encoding genes has been observed in animal and fungi [39].”
BackgroundRegulation of Apoptosis and Autophagy During Anoxia in the Freshwater Crayfish, Faxonius virilis
Breedon, S. A., Gupta, A., & Storey, K. B. (2022) · Marine Biotechnology · doi:10.1007/s10126-022-10132-0 · Cited by 11
“Following this cleavage, Atg8 can be coupled to phosphatidylethanolamine as part of the autophagosome formation mechanism (Shpilka et al. 2011).”
BackgroundAutophagy in the normal and diseased cornea
Teixeira, K. L. D., Gh., M. S., Romano, J., Norouzi, F., & Laurie, G. W. (2022) · Experimental Eye Research · doi:10.1016/j.exer.2022.109274 · Cited by 11
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BackgroundValsa mali effector Vm_04797 interacts with adaptor protein MdAP-2β to manipulate host autophagy
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“This diversi fi cation presumably began with the emergence of multicellular organisms, and subsequent lineage-speci fi c expansions, contractions, and isoform changes have affected the evolution and function of Atg8 across species (39).”
Viral Ubiquitin and Ubiquitin-Like Deconjugases—Swiss Army Knives for Infection
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“The conjugation of UbLs of the LC3/GABARAP family to the membrane lipid phosphatidylethanolamine underlies their involvement in the expansion and fusion of autophagic membranes [25].”
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Claude‐Taupin, A., & Morel, É. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2021.158903 · Cited by 12
Analysis of the Compositional Features and Codon Usage Pattern of Genes Involved in Human Autophagy
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Induction of Autophagy interferes the tachyzoite to bradyzoite transformation ofToxoplasma gondii
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“Atg8 is usually recognized as the most reliable marker for autophagosomes since it is a key and conserved protein for the autophagy (Nakatogawa et al. 2007; Xie et al. 2008; Shpilka et al. 2011; Weidberg et al. 2011).”
BackgroundNeutrophils: Interplay between host defense, cellular metabolism and intracellular infection
Rane, D., Patil, T., More, V., Patra, S. S., Bodhale, N. P., Dandapat, J., & Sarkar, A. (2018) · Cytokine · doi:10.1016/j.cyto.2018.07.009 · Cited by 10
“Under starvation conditions, PI4KIIα localises onto the autophagosomes, interacts with exclusively with GABARAP and GABARAPL2 of Atg8 homologs, [64].”
BackgroundHaghi, M., Masoudi, R., & Najibi, S. M. (2020) · Upsala Journal of Medical Sciences · doi:10.1080/03009734.2020.1785063 · Cited by 10
“These two steps are necessary for elongation and closure of the autophagic membrane (42).”
BackgroundPetraccione, K., Ali, M. G. H., Cyr, N., Wahba, H. M., Stocker, T., Akhrymuk, M., Akhrymuk, I. V., Panny, L., Bracci, N. R., Cafaro, R., et al. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012093 · Cited by 10
“LC3 family members are key mediators of autophagosome formation and elongation in the cytoplasm [60].”
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“LC3-II is then incorporated into the autophagosome membrane, where it is crucial for the recruitment of cargo after binding to adaptor proteins containing the LC3 interacting region (LIR) (Shpilka et al. 2011; Tanida et al. 2004).”
The Ubiquitin Tale: Current Strategies and Future Challenges
Upadhyay, A., & Joshi, V. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00278 · Cited by 11
Relevance of the Exocyst in Arabidopsis exo70e2 Mutant for Cellular Homeostasis under Stress
Neves, J., Monteiro, J., Sousa, B., Soares, C., Pereira, S., Fidalgo, F., Pissarra, J., & Pereira, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010424 · Cited by 9
“The expression of AtATG8, a well-known marker for intracellular autophagy [31]; of AtVTI12, which encodes a protein responsible for the fusion of the vesicles of both EXPO and autophagic pathways with the vacuole; and of AtSYP51, a SNARE involved in the exocytosis process, were evaluated in this mutant background.”
BackgroundZhang, W., Shi, Z., Chen, S., Shen, S., Tu, S., Yang, J., Qiu, Y., Lin, Y., & Dai, X. (2023) · Cell Division · doi:10.1186/s13008-023-00084-9 · Cited by 9
“LC3B is the most studied member of the mammalian ATG8 protein family [31].”
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SARS-CoV2 Nsp3 protein triggers cell death and exacerbates amyloid β42-mediated neurodegeneration
Singh, A. P., Chimata, A. V., Deshpande, P., Bajpai, S., Sangeeth, A., Rajput, M., & Singh, A. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.382989 · Cited by 9
The Role of Autophagy during Development of the Oomycete Pathogen Phytophthora infestans
Luo, Q., Wang, F., Zhong, N., Wang, H., & Xia, G. (2014) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2014.03.004 · Cited by 9
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InfluentialAutophagy: New Questions from Recent Answers
Reggiori, F. (2012) · ISRN Molecular Biology · doi:10.5402/2012/738718 · Cited by 8
“All of them associate with autophagosomes [23, 24].”
BackgroundBerkamp, S., Jungbluth, L., Katranidis, A., Mostafavi, S., Korculanin, O., Lu, P.-H., Ickert, L., Dierig, M. M., Sharma, L., Thukral, L., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-66785-7 · Cited by 12
“The Atg8 family contains ubiquitin-like proteins: Atg8 in yeast and microtubule-associatedprotein1lightchain3(LC3),aswellasgamma-aminobutyric acid type A receptor-associated protein (GABARAP) in mammals 8 .”
Cork cells in cork oak periderms undergo programmed cell death and proanthocyanidin deposition
Inácio, V., Lobato, C., Graça, J., & Morais–Cecílio, L. (2021) · Tree Physiology · doi:10.1093/treephys/tpab031 · Cited by 8
Iron Deficiency and Recovery in Yeast: A Quantitative Proteomics Approach
Navarrete-Perea, J., Guerra-Moreno, Á., Vranken, J. G. V., Isasa, M., Paulo, J. A., & Gygi, S. P. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00035 · Cited by 7
Golpasandi, H., Rahimi, R., Ahmadi, S., Łubkowska, B., & Cięszczyk, P. (2023) · Nutrients · doi:10.3390/nu15184024 · Cited by 8
The Cascade of Oxidative Stress and Tau Protein Autophagic Dysfunction in Alzheimer’s Disease
Liu, Z., Li, P., Wu, J., Wang, Y., Li, P., Hou, X., Zhang, Q., Wei, N., Zhao, Z., Liang, H., et al. (2015) · InTech eBooks · doi:10.5772/59980 · Cited by 9
Nuta, G. C., Gilad, Y., Gershoni, M., Sznajderman, A., Schlesinger, T., Bialik, S., Eisenstein, M., Pietrokovski, S., & Kimchi, A. (2018) · Autophagy · doi:10.1080/15548627.2018.1525476 · Cited by 8
“The Y113 residue is highly conserved in the LC3 protein family, including the closely related members of the GABARAP family of mammalian orthologs of yeast Atg8 (formerly including GABARAPL2/GATE-16 separately, as a family) [12] (Figure 1(b)).”
BackgroundDai, X., Zhou, L., Xu, T., Wang, Q.-Y., Luo, B., Li, Y., Gu, C. J., Li, S., Wang, A.-Q., Wei, W., et al. (2020) · Zoologia (Curitiba) · doi:10.3897/zoologia.37.e52232 · Cited by 9
“LC3 (microtubule-associated protein 1 light chain 3) is a subfamily of essential proteins that contributes to multiple cellular processes, such as autophagy (Shpilka et al. 2011).”
BackgroundInteraction of Poliovirus Capsid Proteins with the Cellular Autophagy Pathway
Zimina, A., Viktorova, E. G., Moghimi, S., Nchoutmboube, J., & Belov, G. A. (2021) · Viruses · doi:10.3390/v13081587 · Cited by 7
“Here we identified a region in the poliovirus structural protein VP0 which was specifically recognized by a commercial monoclonal antibody ag inst a cellular protein LC3A, an Atg8-like protein whose b st-st died function is engagement in the early steps of the autophagosome formati [13,49].”
BackgroundRomano, G., Ibelli, A. M. G., Lorenzetti, W. R., Weber, T., Peixoto, J. D. O., Cantão, M. E., Morés, M. A. Z., Morés, N., Pedrosa, V. B., Coutinho, L. L., et al. (2020) · Genes · doi:10.3390/genes11020117 · Cited by 8
“Moreover, the MAP1LC3C (microtubule‐associated protein 1 light chain 3), one of the top 10 upregulated genes in the affected group, is involved in autophagous processes [40].”
BackgroundMitochondrial dysfunction mediates neuronal cell response to DMMB photodynamic therapy
Gomes, R. D. A. N., Marmolejo-Garza, A., Haan, F.-J., Mitchell, T., Chen, T., Mauthe, M., Parisotto, Y. F., Murakami, M. M., Marie, S. K. N., Baptista, M. S., et al. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119429 · Cited by 7
Walczak, M., Meister, T. R., Nguyen, H. M., Zhu, Y., Besteiro, S., & Yeh, E. (2023) · mBio · doi:10.1128/mbio.03642-21 · Cited by 7
Santos‐Araújo, S., Gomes, F. M., Carvalho‐Kelly, L. F., Meyer‐Fernandes, J. R., Gondim, K. C., & Ramos, I. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1352766 · Cited by 7
Aging and Autophagy: Roles in Musculoskeletal System Injury
Zhang, H., Gu, W., Wu, G., & Yu, Y. (2024) · Aging and Disease · doi:10.14336/ad.2024.0362 · Cited by 7
“In a related study, interactions between six homologous human proteins and 67 other proteins were observed, revealing a large degree of overlap between the members of the family and their potential functions [58].”
Cheung, Y. W. S., Nam, S.-E., Fairlie, G. M. J., Scheu, K., Bui, J. M., Shariati, H. R., Gsponer, J. A., & Yip, C. K. (2024) · Autophagy · doi:10.1080/15548627.2024.2447213 · Cited by 7
“Human cells express six isoforms of Atg8-family proteins that are grouped into the LC3 (MAP1LC3A, MAP1LC3B, MAP1LC3C) and GABARAP (GABARAP, GABARAPL1, GABARAPL2) subfamilies, respectively [23,24].”
Holling, T., Bhavani, G. S., von Elsner, L., Shah, H. H., Kausthubham, N., Bhattacharyya, S. S., Shukla, A., Mortier, G. R., Schinke, T., Danyukova, T., et al. (2022) · Human Mutation · doi:10.1002/humu.24368 · Cited by 7
“LC3B is a mammalian ortholog of Atg8a (Lee & Lee, 2016; Shpilka et al., 2011).”
BackgroundSilva, J. P. E., Furtado, A. P., & dos Santos, J. N. (2014) · International Journal for Parasitology Parasites and Wildlife · doi:10.1016/j.ijppaw.2014.05.004 · Cited by 7
“It is also expressed under a number of stress conditions (Shpilka et al., 2011), for example, in microbial infections, tumour development and food deprivation.”
BackgroundER Stress, UPR and Virus Infections in Plants
Zhang, L., & Wang, A. (2016) · Springer eBooks · doi:10.1007/978-3-319-32919-2_7 · Cited by 7
“2009); (3) vesicle expansion followed by the conjugation of microtubule-associated protein light chain 3 (LC3) with phosphatidylethanolamine (PE) and vesicle completion, represented by the enclosure of cytosolic cargos into double membrane vesicles, leading to the formation of auto-phagosomes (Geng and Klionsky 2008;…”
BackgroundVriend, J. P., & Marzban, H. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2354-3 · Cited by 9
The autophagosome: current understanding of formation and maturation
Lane, J. D., & Mannack, L. (2015) · Research and Reports in Biochemistry · doi:10.2147/rrbc.s57405 · Cited by 8
Chemical approaches to explore ubiquitin-like proteins
Mousa, R., Shkolnik, D., Alalouf, Y., & Brik, A. (2025) · RSC Chemical Biology · doi:10.1039/d4cb00220b · Cited by 6
Mitochondrial proteases and their roles in mitophagy in plants, animals, and yeast
Ludwig, K., & Czarna, M. (2025) · Plant and Cell Physiology · doi:10.1093/pcp/pcaf038 · Cited by 5
“Yeast has a single ATG8 protein (Shpilka et al. 2011), whereas mammals possess six different ATG8 orthologs belonging to the LC3 (microtubule-associated-protein 1 light chain 3) and GABARAP (gamma-aminobutyric acid receptor-associated protein) subfamilies (Onishi et al. 2021).”
Rest, Repair, Repeat: The Complex Relationship of Autophagy and Sleep
Ullern, H., Schnur, P., Boccara, C. N., & Knævelsrud, H. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169227 · Cited by 8
Conserved LIR-specific interaction of Sigma-1 receptor and GABARAP
Baeken, M. W., Christ, M., Schmitt, D., Trein, W., Nagel, H., Clement, A. M., Körschgen, H., & Behl, C. (2025) · iScience · doi:10.1016/j.isci.2025.113287 · Cited by 6
“39,40 They share a primarily cytosolic localization, which changes to a membrane-bound form, both at the inner and outer autophagosomal membrane, upon lipidation.”
Cantharidin downregulates PSD1 expression and inhibits autophagic flux in yeast cells
Swagatika, S., & Tomar, R. S. (2021) · FEBS Open Bio · doi:10.1002/2211-5463.13196 · Cited by 6
“One such key protein involved in autophagosome biogenesis and its subsequent vacuolar fusion is Atg8 (LC3 in mammals) [24, 25].”
BackgroundThe autophagy interaction network of the aging model Podospora anserina
Philipp, O., Hamann, A., Osiewacz, H. D., & Koch, I. (2017) · BMC Bioinformatics · doi:10.1186/s12859-017-1603-2 · Cited by 6
“The ATG8 and LC3 proteins are known to be essential for formation and expansion of the autophagosome membrane during autophagy and to be furthermore crucial for other autophagy-related processes, such as cargo delivery into autophagosomes or for selective targeting of cytosolic components for lysosomal and / or vacuol…”
Yoshimi, A., Hagiwara, D., Ono, M., Fukuma, Y., Midorikawa, Y., Furukawa, K., Fujioka, T., Mizutani, O., Sato, N., Miyazawa, K., et al. (2021) · Frontiers in Fungal Biology · doi:10.3389/ffunb.2021.675459 · Cited by 6
“…and reduction in the number of nuclei were related to autophagy, we constructed strains with the deletion of atgH, which encodes an autophagyrelated ubiquitin-like protein (Shpilka et al., 2011), using the wild-type and CypdA strains (atgH1 and CypdA-atgH1, respectively; Supplementary Figure 11).”
MethodProteomic and metabolomic analysis of Nicotiana benthamiana under dark stress
Shen, J., Chen, Q., Li, Z., Zheng, Q., Xu, Y., Zhou, H., Mao, H., Shen, Q., & Liu, P. (2021) · FEBS Open Bio · doi:10.1002/2211-5463.13331 · Cited by 6
Widyarti, S., Wibowo, S., Sabarudin, A., Abhirama, I., & Sumitro, S. B. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e18123 · Cited by 6
The interaction between DAP1 and autophagy in the context of human carcinogenesis.
Wazir, U., Khanzada, Z. S., Jiang, W. G., Sharma, A. K., Kasem, A., & Mokbel, K. (2014) · PubMed · Cited by 6
Levorin, L., Becker, N., Uluca, B., Gardon, L., Kraus, M., Sevenich, M. M., Apostolidis, A., Schmitz, K., Rüter, N., Apanasenko, I., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c04159 · Cited by 5
miR-137 targets Myc to regulate growth during eye development
Padma, R., Subramanian, M., Chimata, A. V., Rai, A., Yogi, S., Sangeeth, A., Kango‐Singh, M., & Singh, A. (2025) · Development · doi:10.1242/dev.204373 · Cited by 5
“Among these, the Atg8 gene family (Atg8a and Atg8b) has been extensively studied, with its members serving as reliable biomarkers for autophagy (Chimata et al., 2023; Larkin et al., 2021; Shpilka et al., 2011).”
Mammalian innate antiviral defenses: beyond interferon
Rex, E. A., Shaffer, J., Deng, D. M., & Gammon, D. B. (2025) · Journal of Virology · doi:10.1128/jvi.01707-24 · Cited by 7
“2A, Step 2) (111, 112).”
Gu, L., Wang, Y., Xie, S., Liu, Y., Yan, J., Yin, W., & Luo, C. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.04898-22 · Cited by 5
Tepsin binds LC3B to promote ATG9A trafficking and delivery
Wallace, N. S., Gadbery, J. E., Cohen, C. I., Kendall, A. K., & Jackson, L. P. (2024) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-09-0359-t · Cited by 5
“These proteins are further divided into two subfamilies: the LC3 (LC3A/B/C) and GABARAP (GABARAP and GABARAPL1, and GAB-ARAPL2; Shpilka et al. , 2011) families.”
BackgroundWu, F., Deng, L., Wu, X., Liu, H.-B., & Ye, J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122639 · Cited by 5
“However, the autophagy gene Atg8 participates in two ubiquitin similar integration systems and it is the most direct proof to be always used to test the autophagic activity [18].”
BackgroundRobustness of the Autophagy Pathway to Somatic Copy Number Losses
Polo, P., Gremke, N., Stiewe, T., & Wanzel, M. (2022) · Cells · doi:10.3390/cells11111762 · Cited by 5
“The Beclin-1 complex is essential for the nucleation of the phagophore, the immature form of the autophagosome, while vesicle elongation involves the microtubule-associated proteins 1A/1B light chain 3B (MAP1LC3B, also known as ATG8F or LC3), a member of the ATG8 protein family [14].”
BackgroundOh, J., & Tamborindeguy, C. (2023) · Insects · doi:10.3390/insects14020142 · Cited by 5
“For example, sever l ATG8 g nes can be found in mammals, whereas there is o ly a single ATG8 gene in y ast and fungal species [37,38].”
BackgroundMembrane Curvature: The Inseparable Companion of Autophagy
Liu, L., Tang, Y., Zhou, Z., Huang, Y., Zhang, R., Lyu, H., Xiao, S., Guo, D. S., Ali, D. W., Michalak, M., et al. (2023) · Cells · doi:10.3390/cells12081132 · Cited by 5
“Only the completely lipidated Atg8 protein can bind to the IM and participate in the autophagic process [86].”
BackgroundWang, H., Cui, N., Han, W., Su, L., Long, Y., & Liu, D. (2018) · Chinese Medical Journal · doi:10.4103/0366-6999.231522 · Cited by 5
Das, E., Sahu, K. K., & Roy, I. (2023) · FEBS Journal · doi:10.1111/febs.16747 · Cited by 6
mTOR suppresses macroautophagy during postnatal development of the striatumPreprint
Lieberman, O. J., Pigulevskiy, I., Post, M. R., Sulzer, D. L., & Santini, E. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/536680 · Cited by 5
“These molecular events initiate the formation of preautophagic structures that are subsequently expanded by a molecular cascade resulting in the modification of LC3, one of the mammalian homologs of the yeast Atg8 (Shpilka et al., 2011).”
BackgroundSpermidine toxicity in Saccharomyces cerevisiae due to mitochondrial complex III deficiency
Su, W.-H., Smith, J. J., Cheng, E., Nishitani, M. S., Choi, C. Y., Lee, K. R., Salzano, A. P., & Schriner, S. E. (2025) · Biogerontology · doi:10.1007/s10522-025-10233-y · Cited by 4
“It appeared to down-regulate ATG8 , which encodes a protein required for autophagy (Shpilka et al. 2011), and had no effect on ATG33 , which is necessary for mitochondrial specific autophagy (Kanki et al. 2009).”
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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