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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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
Cited by
Sorted by citations
Items 401–500 of 544
Waisner, H., Saud, R., Lasnier, S., Suma, S. M., Foster-Lemieur, K., & Kalamvoki, M. (2025) · mBio · doi:10.1128/mbio.02143-25 · Cited by 4
Parkinson's disease‐linked Kir4.2 mutation R28C leads to loss of ion channel function
Chen, X., Finol‐Urdaneta, R. K., Chen, M., Sykes, A. M., Gao, B., Iqbal, J., Adams, D. J., Mellick, G. D., & Ma, L. (2025) · The Journal of Physiology · doi:10.1113/jp287046 · Cited by 4
“2 protein sequence harbours several LIR (LC3-Interacting Region) motifs, which bind to Atg8/LC3 protein family members to mediate autophagic processes, thereby tagging substrates for autophagy-lysosomal degradation (Geng and Klionsky 2008, Shpilka et al. 2011, Kumar et al. 2022).”
Transcriptomic Changes Predict Metabolic Alterations in LC3 Associated Phagocytosis in Aged Mice
Dhingra, A., Tobias, J. W., Philp, N. J., & Boesze‐Battaglia, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076716 · Cited by 4
“As expected, Map1lc3b was one of the most highly downregulated genes by adjusted p-value; furthermore, there was no compensatory upregulation of a related isoform Map1lc3a (gene encoding for LC3a) or other members of the ATG8/LC3 family (Gabarap, Gabarapl1, Gabarapl2) in the LC3b-/- mouse (Figure 2) [5,28,39-41].”
BackgroundMolecular Mechanism of Autophagy, Cytoplasmic Zoning by Lipid Membranes
Kotani, T., Yasuda, Y., & Nakatogawa, H. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad099 · Cited by 4
Beyond the C-terminal Glycine of ATG8 Proteins – The Story of Some Neglected Amino Acids
Barz, S., Hofmann, K., Reggiori, F., & Kraft, C. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168588 · Cited by 4
γ‐Aminobutyric acid modulates terpene biosynthesis through the ATG8a ‐mediated pathway
Niu, Y., Yang, J., Shi, S., & Yao, T. (2025) · The Plant Journal · doi:10.1111/tpj.70232 · Cited by 4
Studies of Receptor-Atg8 Interactions During Selective Autophagy
Abert, C., & Martens, S. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-8873-0_11 · Cited by 4
Non-canonical roles of ATG8 for TFEB activation
Nakamura, S., Akayama, S., & Yoshimori, T. (2022) · Biochemical Society Transactions · doi:10.1042/bst20210813 · Cited by 6
Chimata, A. V., Darnell, H., Raj, A., Kango‐Singh, M., & Singh, A. (2023) · Autophagy Reports · doi:10.1080/27694127.2023.2252307 · Cited by 4
“Atg8a is the fly ortholog of human LC-3, an important component of autophagy machinery, is involved in phagophore formation, autophagosome formation and autophagolysosome formation, and serves as a reporter for autophagy 40 .”
MITF: an evolutionarily conserved transcription factor in the sea urchin Paracentrotus lividus
Russo, R., Chiaramonte, M., Lampiasi, N., & Zito, F. (2019) · Genetica · doi:10.1007/s10709-019-00077-z · Cited by 4
Berkamp, S., Jungbluth, L., Katranidis, A., Mostafavi, S., Korculanin, O., Lu, P., Sharma, L., Thukral, L., Fitter, J., Dunin‐Borkowski, R. E., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.15.618463 · Cited by 4
Histone deacetylase 6 deacetylates and ubiquitinates ATG3 to regulate autophagy
Yao, J., Zhao, Z., CHEN, Y.-S., Xu, X., Yang, Y., Yue, W., & Shi, X. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01553-0 · Cited by 3
“Acetylated α -tubulin (T7451) and ubiquitin antibody (SAB4503053) were purchased from Sigma-Aldrich.”
Xin, W., Wei, W., Luo, X., Hao, Z., Zhang, L., Zeng, Y.-M., Wan, H., Yang, S., Shang, X., Li, M., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149187 · Cited by 3
ATG gene duplication in vertebrates: evolutionary divergence and its functional implications
Zhang, S., Koyama‐Honda, I., Hiratsuka, D., & Mizushima, N. (2026) · Autophagy · doi:10.1080/15548627.2026.2618126 · Cited by 3
“…[9,10], WDR45B (WD repeat domain 45B) and WDR45 [11,12], and MAP1LC3C (microtubule associated protein 1 light chain 3 gamma; shortened to LC3C hereafter) and GABARAPL2 (GABA type A receptor associated protein like 2) [13,14], many of these duplication events presumably occurred in vertebrates [7].”
Autophagy in the arms race: how pathogen effectors rewire immunity in plants
Yuen, E. L. H., & Bozkurt, T. O. (2026) · Open Biology · doi:10.1098/rsob.250446 · Cited by 3
Pujhari, S. K., Heu, C. C., Brustolin, M., Johnson, R. M., Kim, D., & Rasgon, J. L. (2025) · Autophagy · doi:10.1080/15548627.2025.2523735 · Cited by 5
“Homologs of yeast Atg8 (the MAP1LC3 and GABARAP subfamilies) are another important group of proteins in the autophagy process and act as a marker of autophagy, as they are conjugated to phosphatidylethanolamine and recruited to the phagophore membrane during autophagosome formation [24,25].”
Endomembrane trafficking pathways in Toxoplasma
Besteiro, S., Klinger, C. M., Meissner, M., & Carruthers, V. B. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815041-2.00015-3 · Cited by 3
Zhao, J., Ma, Z., Zheng, H., Huang, Y., Wu, L., Wu, H., Shi, Y., Liu, H., & Liu, Y. (2022) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2022/3534874 · Cited by 3
“LC3II is a mammalian homolog of the yeast autophagy-related protein Atg8 [46] and is the most widely studied molecular marker of autophagosomes.”
BackgroundInhibition of GABARAP or GABARAPL1 prevents aminoglycoside- induced hearing loss
Li, J., Oh, S. I., Liu, C., & Zhao, B. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2416453122 · Cited by 3
“S1 A ) and function redundantly in the autophagy pathway (28).”
Tepsin binds LC3B to promote ATG9A export and delivery at the cell peripheryPreprint
Wallace, N. S., Gadbery, J. E., Cohen, C. I., Kendall, A. K., & Jackson, L. P. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.18.549521 · Cited by 3
“Like yeast ATG8, all mATG8 proteins are conjugated to phosphatidylethanolamine through a ubiquitination-like cascade upon induction of autophagy (Shpilka et al., 2011).”
Two specific interactions of GATE16 with TRPML3 and RAB33B regulate autophagy
Park, J., Choi, A., Kwon, J. S., Choi, S., Park, Y. M., & Kim, H. J. (2025) · Scientific Reports · doi:10.1038/s41598-025-16951-0 · Cited by 2
“Among them, ATG8s divided into two subfamilies, LC3 and GABARAP, play important roles in biogenesis and maturation of autophagosomes 25,26 .”
Atg18 facilitates autophagosome formation via its Atg8‐interacting motif in Saccharomyces cerevisiae
Li, T., Li, X., Li, M., Yuan, T., & Ma, C. (2025) · FEBS Journal · doi:10.1111/febs.70257 · Cited by 2
“The conjugation of Atg8 to phosphatidylethanol-amine (PE) is a crucial step in autophagosome formation in yeast [7 – 9].”
Zeng, R., Liu, Y., Li, Y., Lei, X., Jiang, J., Shen, Q., Ma, Y., Fang, W., & Zhu, X. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms27010235 · Cited by 2
ATG 8 and protein ATG8ylation – more than just A nother T a G ?
Gerth, F., Kosol, S., Aley, N., Agrotis, A., & Ketteler, R. (2026) · Autophagy · doi:10.1080/15548627.2026.2642981 · Cited by 2
“Typically, the members of the ATG8 family have two N-terminal α-helices extending from the ubiquitin-like core [20], which play a role in binding multiple proteins carrying the MAP1LC3/LC3-interacting region (LIR) motif [21].”
Cellular and signaling mechanisms of cyantraniliprole toxicity in the nontarget organism Bombyx mori
Luo, Y., Tang, L., Jing, W., Yang, Y., Ma, H., Pan, M., Lu, Q., Zhou, Y., Li, Y., & Wang, H. (2026) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2026.142404 · Cited by 2
Zhang, Y., Zhou, Q. X., Ke, C., & Huang, H. (2014) · Aquaculture · doi:10.1016/j.aquaculture.2014.05.025 · Cited by 2
Sequence-specific 1H, 15N, and 13C resonance assignments of the autophagy-related protein LC3C
Krichel, C., Weiergräber, O. H., Pavlidou, M., Mohrlüder, J., Schwarten, M., Willbold, D., & Neudecker, P. (2015) · Biomolecular NMR Assignments · doi:10.1007/s12104-015-9633-z · Cited by 2
“Microtubule-associated protein light chain 3C (MAP1LC3C or simply LC3C) is a member of the Atg8 protein family involved inmacroautophagy (Shpilka et al. 2011).”
The Ubiquitin-like Proteins of Saccharomyces cerevisiae
Sengupta, S., & Pick, E. (2023) · Biomolecules · doi:10.3390/biom13050734 · Cited by 3
Multiplex genomic tagging of mammalian ATG8s to study autophagy
Goldin-Azulay, K., Fraiberg, M., Trofimyuk, O., Levin, Y., Reuven, N. B., Kopitman, E., & Elazar, Z. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107908 · Cited by 2
“In yeast, a single Atg8 protein mediates selective and nonselective autophagy, while higher eukaryotes express up to seven family members in mammals and nine in plants (24, 25).”
In silico modeling of the Moniliophthora perniciosa Atg8 protein
Pereira, A. C. F., Cardoso, T. H. S., Brendel, M., & Pungartnik, C. (2013) · Genetics and Molecular Research · doi:10.4238/2013.december.11.13 · Cited by 2
“Later, Atg8p is conjugated to phosphatidylethanolamine (PE) by a covalent bond (Ichimura et al., 2000; Kirisako et al., 2000; Shpilka et al., 2011; Li and Vierstra, 2012), a reaction facilitated by the E3-like Atg12p-Atg5p complex; the conjugated Atg8p can also be de-conjugated by Atg4p (Kirisako et al.”
BackgroundInfluentialXenophagy: Autophagy in Direct Pathogen Elimination
Jo, E., Kim, J. K., & Hwang, S. (2016) · Springer eBooks · doi:10.1007/978-3-319-30079-5_7 · Cited by 2
Multiplexed quantification of autophagic flux by imaging flow cytometry
Montégut, L., Chen, H., Anagnostopoulos, G., Spaggiari, S., Kepp, O., Maiuri, M. C., Kroemer, G., & Martins, I. (2021) · Methods in cell biology · doi:10.1016/bs.mcb.2021.02.005 · Cited by 2
ATG8 is conserved between Saccharomyces cerevisiae and psychrophilic, polar-collected fungi
Ivory, B. J., Smith, H. M., Cabrera, E., Robinson, M. R., Sparks, J. T., Solem, A., Ishihara, J.-I., Takahashi, H., Tsuji, M., & Segarra, V. A. (2021) · PubMed Central · doi:10.17912/micropub.biology.000446 · Cited by 2
“Similarly to that of Sc Atg8, the ubiquitin-like C-terminus of Mb Atg8 consists of a four-stranded β sheet and two α helices (α3 and α4) arranged in a β-grasp fold (Shpilka et al., 2011; Klionsky and Schulman, 2014; Wesch et al., 2020).”
BackgroundInfluentialMethods for measuring autophagy
Andres, A. M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822003-0.00008-5 · Cited by 2
Knepp, B., Ander, B. P., Jickling, G. C., Hull, H., Yee, A., Ng, K., Rodríguez, F., Carmona-Mora, P., Amini, H., Zhan, X., et al. (2022) · Brain Hemorrhages · doi:10.1016/j.hest.2022.04.003 · Cited by 2
“…suppressed in one module in Lobar ICH, and included downregulated SQSTM1 (an autophagy receptor connecting autophagosomes to their cargo), 106 MAP1LC3B (involved in phagophore membrane elongation), 103,107,108 GABARAP, and GABARAPL2 (both involved in late stage autophagosome formation).”
NUCLEAR RETENTION OF LEPTIN/UPD2 REGULATES ORGANISMAL RESILIENCE TO NUTRIENT EXTREMESPreprint
Poling, M. E., Sullivan, C. E., Madan, A., Kelly, K., Brent, A. E., Dubrulle, J., Raghavan, P., & Rajan, A. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.29.428913 · Cited by 2
“We postulated that Atg8, a ubiquitin-like protein (Shpilka et al., 2011), might operate akin to other ubiquitin and ubiquitin-like proteins that have been shown to function in cellular localization [70–72].”
BackgroundSystematic Analysis of Autophagy Identifies Atg9 Vesicles as the Origin of the PhagophorePreprint
Broadbent, D. G., Barnaba, C., & Schmidt, J. C. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.03.502680 · Cited by 2
“, 2019), which acts similarly to ubiquitin ligase complexes but instead conjugates LC3/GABARAP proteins to phosphatidylethanolamine at the autophagosome membrane (Kirisako et al., 1999; Shpilka et al., 2011).”
BackgroundAF2-multimer guided high accuracy prediction of typical and atypical ATG8 binding motifsPreprint
Ibrahim, T., Khandare, V. S., Mirkin, F. G., Tümtaş, Y., Bubeck, D., & Bozkurt, T. O. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.25.509395 · Cited by 2
“Many of these proteins are also conserved in plants and humans, such as the ubiquitinlike ATG8-family proteins that play central roles in virtually all steps of autophagy, from cargo sequestration to transport and lysosomal fusion of autophagosomes [5, 6].”
BackgroundGABA-mediated inhibition in visual feedback neurons fine-tunes Drosophila male courtship
Mabuchi, Y., Cui, X., Xie, L., Kim, H., Jiang, T., & Yapici, N. (2023) · doi:10.1101/2023.01.25.525544 · Cited by 1
“GABARAP (also known as Atg8a) belongs to a family of ubiquitin-like proteins that regulate multiple intracellular processes, including autophagy (Martens and Fracchiolla, 2020; Mizushima, 2020; Shpilka et al., 2011).”
BackgroundInfluentialShalev, I., Somekh, J., & Eran, A. (2021) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2021-108193 · Cited by 1
Role of Autophagy in the Occurrence and Development of Atherosclerosis Induced by Low Shear Stress
王, 志. (2022) · Advances in Clinical Medicine · doi:10.12677/acm.2022.12121632 · Cited by 1
Li, R., & Huang, Y. K. (2024) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2024.110227 · Cited by 1
Meng, Y., Lv, L., Yao, H., Lin, Z., & Dong, Y. (2025) · Animals · doi:10.3390/ani15060795 · Cited by 1
“This phenomenon has been reported across multiple gene families [50,51].”
Liao, D., Chen, W., Deng, Y., Wei, S., Wang, L., & Hu, J. (2025) · Eye and Vision · doi:10.1186/s40662-025-00448-y · Cited by 1
“The C-terminal residues of ATG8-family of proteins undergo ubiquitin-like conjugation with the lipid phosphatidy-lethanolamine on the phagophore membrane, which is necessary for autophagy membrane elongation together with autophagosome maturation and closure processes [25].”
High-fat diet impairs intermediate-term memory by autophagic-lysosomal dysfunction in Drosophila
Tong, Y. A., Jiang, M., Onuki, K., Itoh, M., & Tonoki, A. (2025) · PLoS Genetics · doi:10.1371/journal.pgen.1011818 · Cited by 1
The AP-4 accessory protein tepsin exhibits multivalent binding to LC3B
Cohen, C. I., Kendall, A. K., Wallace, N. S., McCorkle, M., & Jackson, L. P. (2025) · Advances in Biological Regulation · doi:10.1016/j.jbior.2025.101124 · Cited by 1
“LC3B is a member of the mammalian ATG8 (mATG8) family and orthologue of the yeast autophagy protein, ATG8 (Wallace et al., 2024; Feng et al., 2014; Shpilka et al., 2011).”
Deubiquitinase MoAMSH inhibits autophagy by targeting MoAtg6 in Magnaporthe oryzae
Liao, J., Shen, Z.-F., Wang, J.-Y., He, M.-F., Lv, H.-M., Zhao, J., Zhang, Y., Zhu, X., Li, L., Wang, Z., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02487-3 · Cited by 1
Men, Y. N., Chen, J. N., Cai, H., & Yang, C. N. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl45346 · Cited by 2
Yu, S.-F., Kimaro, J. P., Zhou, X., Li, S., Zheng, L., & Chang-Feng, C. H. I. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-11467-w · Cited by 1
Liao, J., Shen, Z.-F., Wang, J.-Y., He, M., Lv, H.-M., Zhao, J., Zhao, W., Li, L., Wang, Z., Sun, L., et al. (2026) · Microbiological Research · doi:10.1016/j.micres.2026.128479 · Cited by 1
Ubiquitin-like modifications in adipose tissue development and obesity: New insights
Chakraborty, S., & Chen, W. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2026.168234 · Cited by 1
CHCHD2 and CHCHD10 promoted autophagic clearance of protein aggregates via GABARAPs
Wei, Z., Zhang, M. M., Tang, W., Singh, B. K., Zhiwei, Z., Lei, Z., Wee, J. G. K., En, F. T. R., Jingxiu, H., Sun, Q., et al. (2026) · Autophagy · doi:10.1080/15548627.2026.2678427 · Cited by 1
“ATG8s are present mostly in the cytosol and sometimes in mitochondria [75].”
GlRac regulates an ATG8-independent autophagy-like pathway in Giardia lamblia
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) · PLoS Pathogens · doi:10.1371/journal.ppat.1014624 · Cited by 1
“…to S. cerevisiae ATG8 ( Sc ATG8), the Giardia protein lacks the four β -strands that form the ubiquitin-like core required for ATG8 function [71,72] (S7B Fig), yielding a high root-mean-square deviation (RMSD, a standard measure of structural similarity in which lower values indicate greater…”
Survey of the human proteostasis network: the autophagy-lysosome pathway
Powers, E. T., Elsasser, S., Tan, E. P., Cole, C. M., Xiao, Q., Stoeger, T., Sui, X., Kurtzbard, R. D., Martínez-Botía, P., Richardson, R. A. K., et al. (2026) · Autophagy · doi:10.1080/15548627.2026.2741038 · Cited by 2
Li, Z., Xin, J., Chen, W., Liu, J., Zhu, M., Zhao, C., Yuan, J., Jin, G., Ma, H., Du, J., et al. (2017) · Gene · doi:10.1016/j.gene.2017.05.017 · Cited by 1
Autophagic Proteases: Functional and Pathophysiological Aspects
Pramanik, P. K., Paik, D., Pramanik, A., Alam, M. N., Das, P., & Chakraborti, T. (2017) · Springer eBooks · doi:10.1007/978-981-10-3162-5_14 · Cited by 1
Boyer‐Guittaut, M., Varambally, S., Darley-Usmar, V. M., & Zhang, J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.10.163 · Cited by 1
Dicer promotes Atg8 expression through RNAi independent mechanism in Cryptococcus neoformans
Feng, W., Yang, M., Li, X., & Wei, D. (2021) · FEMS Yeast Research · doi:10.1093/femsyr/foab037 · Cited by 1
Proteolytic processing in autophagy
Machado‐Neto, J. A., & Leitão, A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-85696-6.00011-1 · Cited by 1
Crosstalk between Autophagy and Apoptosis in Intervertebral Disc Degeneration
Saciloto, B., Nicoletti, N. F., Peletti-Figueiró, M., & Falavigna, A. (2021) · Journal of Biosciences and Medicines · doi:10.4236/jbm.2021.912003 · Cited by 1
“In mammalian cells, LC3 is expressed in multiple isoforms: LC3A, LC3B, and LC3C [13] [19].”
BackgroundVacuolar Proteases of Candida auris from Clades III and IV and Their Relationship with Autophagy
Clark-Flores, D., Vidal-Montiel, A., Mondragón‐Flores, R., Valentı́n, E., Hernández-Rodríguez, C., Juárez‐Montiel, M., & Villa‐Tanaca, L. (2025) · Journal of Fungi · doi:10.3390/jof11050388 · Cited by 1
“Additionally, under these conditions, we also observed overexpression of the gene encoding the Atg8 protein, which is noteworthy because Atg8 is commonly used as a marker of autophagy in yeast cells [68].”
Rayevsky, A. V., Bulgakov, E., Stykhylias, M., Ozheredov, S. P., Spivak, S. I., & Blume, Y. B. (2025) · Molecular Informatics · doi:10.1002/minf.70004 · Cited by 1
“Yeast has a single ATG8 protein [11, 37].”
Santos, R. D. S. (2013) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.17.2013.tde-15052014-104035 · Cited by 1
Taniguchi, S., Toyoshima, M., Takamatsu, T., & Mima, J. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/870857 · Cited by 1
“Atg8-like domain, exhibiting 30-35% (for the LC3 proteins) and 54-56% (for the GABARAP proteins) sequence identities to Atg8p in yeast (Figure 1A, B; Figure S1) [26].”
BackgroundInfluentialThe sumoylation and neddylation networks in Aspergillus nidulans development
Harting, R. (2013) · doi:10.53846/goediss-4105 · Cited by 1
Pujhari, S. K., Heu, C. C., Brustolin, M., Johnson, R. M., Kim, D., & Rasgon, J. L. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.02.526867 · Cited by 1
Bulgakov, E., Rayevsky, A. V., Blume, Y. B., Karpov, P. A., Stykhylias, M., Ozheredov, S. P., & Spivak, S. (2024) · Research Square · doi:10.21203/rs.3.rs-4831294/v1 · Cited by 1
A dinoflagellate-infecting giant virus with a micron-length tailPreprint
Gajigan, A. P., Schvarcz, C. R., Laughlin, A., Weatherby, T. M., Culley, A. I., Edwards, K. F., & Steward, G. F. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.19.665647 · Cited by 1
“Another autophagy-related gene encoded by PelV-1, Atg8, is a key component in the formation of autophagosomes (Shpilka et al., 2011).”
Cell Autophagy and Myocardial Ischemia/Reperfusion Injury
Zhang, S., Wang, J., Du, Y., Shang, J., Wang, L., Wang, J., Wang, K., Bai, K., Lv, T., Li, X., et al. (2013) · InTech eBooks · doi:10.5772/53442 · Cited by 2
Kyöstilä, K. (2015) · Työväentutkimus Vuosikirja
Defining the role of folliculin and its interacting partners
Seifan, S. (2016) · ORCA Online Research @Cardiff (Cardiff University)
Lassen, A. D. (2013) · ResearchWorks at the University of Washington (University of Washington)
Autophagy in siRNA-mediated PRKAR1A knockdown canine osteosarcoma cells
Wong, J. K. (2016) · The Atrium (University of Guelph)
Divergent Roles of Atg8 Orthologues in Autophagy
Mathur, A. (2015) · Biochemistry & Pharmacology Open Access · doi:10.4172/2167-0501.1000e177
BioID indicates the involvement of the TRAPP protein TrappC11 in autophagy
Zhao, Q. (2016) · Spectrum Research Repository (Concordia University)
The Role of the Small Rab24 GTPase in Autolysosome Clearance
Honkanen, R. (2016) · Työväentutkimus Vuosikirja
Physiology Directed Drug Discovery in Multidrug Resistant Plasmodium falciparum
Siriwardana, A. (2017) · DigitalGeorgetown (Georgetown University Library)
Role of alveolar epithelial cells in macrophage responses against mycobacterial infections
Flores, C., & Daniela, O. (2013)
Targeting Unselective Autophagy of Cellular Aggregates
Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801944-3.00004-7
“Among them, the complex centered around Atg8-like UBL proteins, such as the light chain 3 (LC3) protein [18].”
BackgroundUnselective Disposal of Cellular Aggregates
Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800186-8.00004-3
Mitter, A. L. (2018) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-6801
Biochemical and Structural Characterization of the Atg8/LC3 Lipidation Pathway
Zheng, Y. (2020) · doi:10.21007/etd.cghs.2020.0499
“…proteins in higher eukaryotes, here referred collectively to Atg8 family members) and the E1-E2-E3 enzymatic cascade that links Atg8’s C-terminus to the primary amine group of phosphatidylethanolamine (PE) lipid molecules (Dikic, 2017; Ichimura et al., 2000; Shpilka et al., 2011, 2012).”
BackgroundIntraperitoneal injection of ketamine enhances apoptosis in urothelium via autophagy in rats
Wei, L., Wu, J., Li, D., & Shan, Z. (2020) · European Journal of Inflammation · doi:10.1177/2058739220935661
Walczak, M., Meister, T. R., Zhu, Y., & Yeh, E. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.24.445495
“4 protists has expanded to multiple Atg8 paralogs in mammals and plants, hypothesized 68 to represent functional specialization and diversification (7).”
BackgroundSønstevold, T. (2021) · NORA - Norwegian Open Research Archives
Robustness of the autophagy pathway to somatic copy number lossesPreprint
Polo, P., Gremke, N., Stiewe, T., & Wanzel, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.29.489531
Deretic, V. P. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733643363.793549028
Wang, Y., & Huang, S. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.726018759.793539019
Molinari, M., & Loi, M. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733643363.793551952
Inhibition of Autophagy by a Small Molecule through Covalent Modification of the LC3 Protein
Fan, S., Yue, L., Wan, W., Zhang, Y., Zhang, B., Otomo, C., Li, Q., Lin, T., Hu, J., Xu, P., et al. (2021) · Angewandte Chemie · doi:10.1002/ange.202109464
Noncanonical Phosphoproteomics – II
(2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839162312-00490
Role of Ubiquitin in the Survival of Legionella pneumophila in Eukaryotic Host Cells
Wang, S. J. (2017) · McGill Science Undergraduate Research Journal · doi:10.26443/msurj.v12i1.44
“(61) Functionally, LC3-II has been observed to facilitate autophagosomal membrane expansion.”
BackgroundAnalysis of ATG8 Family Members Using LC3-Interacting Regions (LIR)-Based Molecular Traps
Quinet, G., Génin, P., Belgareh‐Touzé, N., Ozturk, O., Weil, R., Cohen, M. M., Legouis, R., & Rodríguez, M. S. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2859-1_14
A Drosophila Arl8 kis GTPáz szerepe a lizoszomális fúziós folyamatokban
Boda, A. (2020) · Eötvös Loránd Tudományegyetem · doi:10.15476/elte.2020.141
TaATG8 is involved in the response to abiotic stresses and powder mildew in ArabidopsisPreprint
Tian, L., Wang, D., Liu, G., Wei, F., Hou, C., Han, S., & Zhang, F. (2023) · Research Square · doi:10.21203/rs.3.rs-2838851/v1
Atg8-LC3 controls systemic nutrient surplus signaling from flies to humansPreprint
Madan, A., Kelly, K., Sullivan, C. E., Poling, M. E., Brent, A. E., Alassaf, M., Dubrulle, J., & Rajan, A. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.31.543119
ATG8 family protein, cargo selection, and autophagy
Mishra, A., & Dhiman, R. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-90142-0.00006-2
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
