The DOI matches its Crossref record; 114 of the 115 references it cites were found in a registry or an index.
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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Citations
Cites
The Pfam Protein Families Database
Bateman, A. G. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.276 · Cited by 14,075
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 · cited 1×
“Although mammalian Atg8 proteins were originally implicated in intracellular trafficking processes, they are all found within autophagosomes [73-75].”
BackgroundPankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578 · cited 1×
“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].”
BackgroundSequence logos: a new way to display consensus sequences
Schneider, T. D., & Stephens, R. M. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.20.6097 · Cited by 3,354 · cited 1×
“[113] show the conservation (overall height) and residue prevalence of multiple alignment positions.”
BackgroundBjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276 · cited 2×
“These adaptors bind simultaneously to Atg8 proteins and to ubiquitinated proteins, organelles, and in some cases pathogens [18,94,103].”
BackgroundCDD: a Conserved Domain Database for the functional annotation of proteins
Marchler‐Bauer, A., Lu, S., Anderson, J. B., Chitsaz, F., Derbyshire, M. K., DeWeese-Scott, C., Fong, J. H., Geer, L. Y., Geer, R. C., Gonzales, N. R., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1189 · Cited by 3,126 · cited 2×
“Sequences for the alignments were taken from the CDD [114] and PFAM [115] database entries cd01611 and PF02991, respectively, and sequences”
MethodThe Pfam protein families database
Finn, R. D., Mistry, J., Tate, J., Coggill, P., Heger, A., Pollington, J. E., Gavin, O. L., Gunasekaran, P., Ceric, G., Forslund, K., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp985 · Cited by 2,694 · cited 2×
“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
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 · cited 2×
“Unlike ubiquitin, which is conjugated to a protein, Atg8 is covalently conjugated to PE lipid through its carboxy-terminal exposed glycine [64].”
BackgroundMizushima, N., Yamamoto, A., Matsui, M., Yoshimori, T., & Ohsumi, Y. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0704 · Cited by 2,105 · cited 1×
“Thus, transgenic mice and tissue-culture cells expressing GFP-LC3 have been used to investigate autophagy [84,85].”
BackgroundReactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
Scherz‐Shouval, R., Shvets, E., Fass, E., Shorer, H., Gil, L., & Elazar, Z. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601623 · Cited by 2,101 · cited 1×
“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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Items 501–544 of 544
A new cellular platform for studying autophagyPreprint
Goldin-Azulay, K., Fraiberg, M., Trofimyuk, O., Levin, Y., Reuven, N. B., Kopitman, E., & Elazar, Z. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.28.587157
“Current autophagy studies primarily rely on ectopically expressed Atg8s, which may falsely modulate the autophagic flux [25] or form an autophagy-independent aggregates [28].”
BackgroundBrennan, A., Oldham, N. J., Layfield, R., & Scott, D. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-4067-8_19
Chaudhary, M., Soni, N., Dongre, S., Tiwari, A., Malik, N., Chosdol, K., & Bissa, B. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.17.618809
“The ATG8 family has 8 orthologs; LC3A, LC3B, LC3B2, LC3C (encoded by Microtubule-Associated Protein-1 Light Chain-3 or MAP1LC3), and γ-aminobutyric acid receptor-3 associated protein (GABARAP), GABARAPL1 (GABARAP like protein 1), GABARAPL2 (also known as GATE-16), and GABARAPL3 7,8 .”
TaATG8 Is Involved in the Response to Abiotic Stresses and Powdery Mildew in Arabidopsis
Tian, L. J., Liu, G., Wang, R., Wei, F., Zhang, F. F., Hou, C. Y., & Wang, D. M. (2024) · Russian Journal of Genetics · doi:10.1134/s1022795424700893
“Most of the autophagy proteins perform function in unique way in the process of forming the autophagic body [7], and some of them are used as the maker protein, such as ATG8 [8].”
Chaudhary, M., Soni, N., Malik, N., Chosdol, K., & Bissa, B. (2025) · Tissue and Cell · doi:10.1016/j.tice.2025.102991
Functional Analysis of the Autophagy-Related Gene OsATG4b in Rice Grain Chalkiness Regulation
Hu, Z. Q., Han, X., Yuan, Y., Xing, R., Liu, H., Li, C., Shen, H., Guo, Y., Sun, S., Yang, Y., et al. (2025) · Plants · doi:10.3390/plants14162530
“Specifically, the covalent linkage of ATG8 to the membrane lipid phosphatidylethanolamine (PE) is a critical step required for autophagosome expansion and maturation [23–25].”
Retinal proteomics in neurodegeneration: Insights into ocular and brain disorders
Mirshahvaladi, S., Gaire, B. P., Kashani, S. A., Guha, A., Koronyo, Y., Fuchs, D.-T. S., You, Y., Black, K. L., Paulo, J. A., Graham, S. L., et al. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00291
“Dysfunctional cerebral autophagy in AD was reported to lead to the accumulation of misfolded proteins such as Aβ and tau, promoting neurodegeneration (Shpilka et al., 2011; Zhang et al., 2021).”
Recent advances in glycosome biogenesis and its implications for drug discovery
Hohnen, L., Krishna, C. K., Walker, L., Erdmann, R., & Kalel, V. C. (2025) · Biological Chemistry · doi:10.1515/hsz-2025-0183
“While there is only one ATG8 gene in yeast and fungi, higher eukaryotes and kinetoplas-tids contain several (Shpilka et al. 2011).”
Fu, Z., Li, X., El‐Aty, A. M. A., Yagan, R., Ju, X., & Yong, Y. (2025) · Veterinary Sciences · doi:10.3390/vetsci12121200
“Notably, at this fusion stage, ATG14L in the Beclin 1-VPS34 complex is replaced by UV resistance-associated gene protein (UVRAG) [19,20].”
Klińska, S., Kędzierska, S., Demski, K., & Banaś, A. (2023) · Figshare · doi:10.6084/m9.figshare.23751826
Mariño, G., Tamargo‐Gómez, I., García, R., Martínez-García, G. G., Suárez, M. F., Cimadevilla, O. C. F., Caravia, X. M., Pérez, R. F., Rey, V., Calvo, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.29.678527
Mondal, P., Cyril, A., Mamriev, D., Parham, L. R., Wierzbicki, I. H., Shen, C., Doglioni, G., Dufrense, S., Komarla, A., Gonzalez, D. J., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.03.703609
“Subsequently, two ubiquitin-like conjugation systems facilitate the lipidation of ATG8 family proteins, including GABA type A Receptor-Associated Proteins (GABARAPs) and Microtubule-Associated Protein 1 Light Chain 3 (MAP1LC3) 23, 24 .”
Gl Rac regulates an ATG8-independent autophagy-like pathway in Giardia lambliaPreprint
Klippel, A. H., Newman-Boulle, C., Reed, G., Dule, D., Kedia, S., Kelty, M. T., Chan, W. P., Shih, H.-W., & Paredez, A. R. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.17.706457
Implication du suppresseur de tumeur TP53INP1 dans l'autophagie et le métabolisme lipidique
Seillier, M. (2013) · theses.fr (ABES) · doi:10.70675/db061acdz0fddz4d26z87c9zdc0750155617
Khalil, B. (2016) · theses.fr (ABES) · doi:10.70675/4446111fz4182z4737zae76z7f117887a893
Alfaisal, J. (2016) · theses.fr (ABES) · doi:10.70675/912b4531z9f61z4aacz89bez526a9131ecb9
Modulation de l'autophagie neuronale par la sérine protéase tPA en conditions ischémiques
Thiebaut, A. M. (2019) · theses.fr (ABES) · doi:10.70675/6586c0abz9e4cz455fz95ffzc52ec76397f8
Functional characterisation of Drosophila M1BP
Barthez, M. (2019) · theses.fr (ABES) · doi:10.70675/38635cdczfedaz4361zb0a3z7b6850e707ed
Gonzalez-Santamarta, M. (2022) · theses.fr (ABES) · doi:10.70675/7321c487z9a40z470eza548zb4a43e4d0322
Gökerküçük, E. B. (2022) · theses.fr (ABES) · doi:10.70675/5292e3e3z57efz4337z9710z536ed06cf7fb
Upadhayay, K., Bhardwaj, P., Farooqi, N., Rabha, B., Mishra, A., Verma, K., Singh, R., & Sharma, D. (2026) · Autophagy · doi:10.1080/15548627.2026.2654191
“To inhibit macroauto-phagy, we deleted ATG8 which is crucial for the process [25,26].”
Moon, S., Lee, S., & Choi, Y. (2026) · Development & Reproduction · doi:10.12717/dr.2026.30.1.25
“LC3 is involved in autophagosome formation and autophagy selection in the cytoplasm, and is one of the most widely used markers of autophagy (Shpilka et al., 2011; Wild et al., 2014).”
Meligy, F. Y., Elghait, A. T. A., el‐Rady, N. M. A., Kamel, A. A., & Gameaa, F. K. (2026) · Ultrastructural Pathology · doi:10.1080/01913123.2026.2650192
“38,39 According to Kabeya et al., 40 LC3-I is cytosolic, while LC3-II, the lapidated form, is membrane bound.”
Hui, L. I., Yu, D. I. N. G., & Xie, Z. (2026) · Scientia Sinica Vitae · doi:10.1360/ssv-2026-0054
Lee, J.-Y., Bai, J.-S., Li, Y., Jung, W., Je, J., & Lee, S.-J. (2026) · Toxicon · doi:10.1016/j.toxicon.2026.109147
Atg8 orchestrates stress-responsive chromatin programs across immunity and metabolismPreprint
Kelly, K., Ramesh, N. A., Ranganathan, S., Madan, A., Marschall, S., Unckless, R. L., & Rajan, A. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.22.727304
“Atg8 is best known for its canonical role in macroautophagy, where covalent conjugation to phosphatidylethanolamine (PE) anchors Atg8 onto nascent autophagosomal membranes and supports cargo selection, autophagosome maturation, and lysosomal turnover during nutrient scarcity[8-11].”
Virulensome: a transient organelle mediating fungal virulence
Zhao, P., Hu, Q.-Y., Wang, S.-H., Wang, C.-S., Jian, X.-X., Wen, X.-F., Luo, Y., Zhang, Y.-Q., Xiang, C., Li, G.-H., et al. (2026) · Science China Life Sciences · doi:10.1007/s11427-026-3388-2
“Classic examples include autophagosomes, which safeguard homeostasis under stress (Mizushima et al., 1998; Shpilka et al., 2011; Wang et al., 2023), and more recently discovered entities such as migrasomes (Fan and Chen, 2026; Ma et al., 2015), PXo body (Xu et al., 2023), nitroplast (Coale et al.,…”
Role of ubiquitin-like proteins in plant pathogen interactions
Devi, K., Sood, P., & Prasad, A. (2026) · Physiological and Molecular Plant Pathology · doi:10.1016/j.pmpp.2026.103362
Tsong, H., Rodriguez, M. N., & Stavoe, A. K. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.15.738464
“Lipidated Atg8 appears to be involved in many steps of autophagy, including phagophore membrane extension, membrane tethering, cargo recognition, autophagosome transport, and lysosomal fusion (Shpilka et al. 2011; Lystad and Simonsen 2019).”
Zheng, Z., Huang, Z., Liu, S., Lin, Q., Zhao, N., Zhang, H., & Zheng, H. (2026) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2026.105715
Dealing with membrane stress through CASM
Haukaas, H. S., Carlsson, S. R., & Lystad, A. H. (2026) · Autophagy · doi:10.1080/15548627.2026.2717033
Jo, S. H., Moon, J. Y., Jung, S., Lim, G., Kachroo, P., & Park, J. M. (2026) · Molecular Plant Pathology · doi:10.1111/mpp.70350
“The functional diversification of the ATG8 family in plants may provide multiple interfaces through which viral proteins interact with autophagy-associated pathways (Kellner et al. 2017; Shpilka et al. 2011).”
ATG4B-dependent processing of tandem-domain BmLC3 exposes a Tyr136-regulated C-terminal fragment
Shin, W.-D., Kim, H.-J., Ma, S.-H., Park, S.-W., Jun, Y., Lee, D.-K., Hwang, I., Jang, D., & Lee, J.-A. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1957836
“Membrane-bound ATG8 proteins contribute to autophagosome expansion, closure, cargo recruitment, and membrane dynamics (Ichimura et al., 2000; Shpilka et al., 2011; Maruyama and Noda, 2018; Nakatogawa, 2020).”
BindingDB (2022) · UC San Diego · doi:10.7270/q2m90dbr
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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