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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
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.
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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”
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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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“Thus, transgenic mice and tissue-culture cells expressing GFP-LC3 have been used to investigate autophagy [84,85].”
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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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Items 101–200 of 544
Regulation of ATG and Autophagy Initiation
Li, W., & Zhang, L. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-0602-4_2 · Cited by 72
ERES: sites for autophagosome biogenesis and maturation?
Sánchez, J., Ktistakis, N. T., & Reggiori, F. (2015) · Journal of Cell Science · doi:10.1242/jcs.158758 · Cited by 68
“…intermediate compartment are necessary and sufficient to catalyze the in vitro lipidation of LC3, which is essential for autophagosome formation (Shpilka et al., 2011), and that these membranes lose this capacity when ER-to-Golgi transport inhibitors are added to the in vitro LC3 lipidation…”
BackgroundInfluentialMacroautophagy and Chaperone‐Mediated Autophagy in Heart Failure: The Known and the Unknown
Ghosh, R., & Pattison, J. S. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/8602041 · Cited by 72
“GABARAP subfamily [222] GABARAP/ATG8A GABARAPL1/GEC1/ATG8B GABARAPL2/GATE16/”
MethodThe role of chloroplasts in plant pathology
Sowden, R. G., Watson, S. J., & Jarvis, P. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170020 · Cited by 69
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, J., Abeliovich, H., Acevedo‐Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Kölner Universitäts PublikationsServer (Universität zu Köln) · doi:10.5167/uzh-131237 · Cited by 69
Regulation of ATG8 membrane association by ATG4 in the parasitic protistToxoplasma gondii
Kong-Hap, M., Mouammine, A., Daher, W., Berry, L., Lebrun, M., Dubremetz, J., & Besteiro, S. (2013) · Autophagy · doi:10.4161/auto.25189 · Cited by 68
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BackgroundWu, H., Pu, J., Krafft, P. R., Zhang, J., & Chen, S. (2014) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-014-0116-z · Cited by 72
The Evolution of the Hallmarks of Aging
Lemoine, M. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.693071 · Cited by 76
“Regarding autophagy, there are only studies of the conservation of proteins involved, like Atg8 (Shpilka et al., 2011).”
BackgroundJiang, T.-X., Zou, J.-B., Zhu, Q.-Q., Liu, C. H., Wang, G., Du, T., Luo, Z.-Y., Guo, F., Zhou, L., Liu, J., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1901039116 · Cited by 69
AlphaFold2-multimer guided high-accuracy prediction of typical and atypical ATG8-binding motifs
Ibrahim, T., Khandare, V. S., Mirkin, F. G., Tümtaş, Y., Bubeck, D., & Bozkurt, T. O. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3001962 · Cited by 61
“Many of these proteins are also conserved in plants and humans, such as the ubiquitin-like 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].”
Lieberman, O. J., & Sulzer, D. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.028 · Cited by 66
“Mammals have numerous Atg8 homologs, including the LC3 and GABARAP families [51].”
BackgroundReggiori, F., Komatsu, M., Finley, K. D., & Simonsen, A. (2012) · International Journal of Cell Biology · doi:10.1155/2012/156272 · Cited by 68
“It has to be noted that mammals possess at least 7 genes coding for LC3/Atg8 proteins that can be grouped into three subfamilies: (1) the LC3 subfamily containing LC3A, LC3B, LC3B2 and LC3C; (2) the gammaaminobutyrate receptor-associated protein (GABARAP) subfamily comprising GABARAP and GABARAPL1 (also called GEC1);…”
BackgroundLipid Geometry and Bilayer Curvature Modulate LC3/GABARAP-Mediated Model Autophagosomal Elongation
Landajuela, A., Hervás, J. H., Antón, Z., Montes, L. R., Gil, D., Valle, M., Rodriguez, J. F., Goñi, F. M., & Alonso, A. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2015.11.3524 · Cited by 69
Borel, S., Robert-Hebmann, V., Alfaisal, J., Jain, A., Faure, M., Espert, L., Chaloin, L., Paillart, J., Johansen, T., & Biard‐Piechaczyk, M. (2014) · AIDS · doi:10.1097/qad.0000000000000554 · Cited by 74
“Mammals have six ATG8-like proteins (mATG8s) that comprise three microtubule-associated protein 1 light chain 3 (LC3) proteins (LC3A, B, and C), one gamma-aminobutyrate receptor-associated protein (GABARAP) and two GABARAP-like proteins (GABARAPL1 and GATE16/GABARAPL2) [3].”
BackgroundSeo, E., Woo, J., Park, E., Bertolani, S. J., Siegel, J. B., Choi, D., & Dinesh‐Kumar, S. P. (2016) · Autophagy · doi:10.1080/15548627.2016.1217373 · Cited by 64
Cross talk between autophagy and oncogenic signaling pathways and implications for cancer therapy
Zada, S., Hwang, J. S., Ahmed, M., Lai, T. H., Pham, T. M., Elashkar, O., & Kim, D. R. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188565 · Cited by 65
Cheng, X., Wang, Y., Gong, Y., Li, F., Guo, Y., Hu, S., Liu, J., & Pan, L. (2016) · Autophagy · doi:10.1080/15548627.2016.1185590 · Cited by 62
Gao, S., Zhang, S., Zhou, H., Tao, X., Ni, Y., Pei, D., Kang, S., Yan, W., & Lu, J. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.628541 · Cited by 63
“Con, control group; Con+Rapa, control group with rapamycin pretreatment; A/S, anesthesia/surgery group; A/S+Rapa, anesthesia/surgery group combined with rapamycin pretreatment. expression of LC3-II is regarded as a marker of the activity of autophagy (Shpilka et al., 2011).”
MethodGorovits, R., & Czosnek, H. H. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.00355 · Cited by 62
“Proteins destined for degradation are attached to ubiquitin (Ub) and this complex is then degraded by the 26S proteasome, the major proteolytic system of eukaryotic cells (Voges et al., 1999; Smalle and Vierstra, 2004; Sadanandom et al., 2012).”
BackgroundYe, J., Zou, G., Zhu, R., Kong, C., Miao, C., Zhang, M., Li, J., Xiong, W., & Wang, C. (2021) · Nature Communications · doi:10.1038/s41467-020-20624-z · Cited by 61
Zheng, Y., Qiu, Y., Grace, C. R., Liu, X., Klionsky, D. J., & Schulman, B. A. (2019) · Nature Communications · doi:10.1038/s41467-019-11435-y · Cited by 61
ISG15 Connects Autophagy and IFN-γ-Dependent Control of Toxoplasma gondii Infection in Human Cells
Bhushan, J., Radke, J. B., Perng, Y.-C., McAllaster, M. R., Lenschow, D. J., Virgin, H. W., & Sibley, L. D. (2020) · mBio · doi:10.1128/mbio.00852-20 · Cited by 64
“, GABARAP, GABARAPL1, and GATE-16 [also known as GABARAPL2]), while mice express five related proteins (LC3a, LC3b, Gabarap, Gabarapl1, and Gate-16) (68, 69).”
BackgroundMammalian Atg8 proteins regulate lysosome and autolysosome biogenesis through SNAREs
Gu, Y., Abudu, Y. P., Kumar, S. G., Bissa, B., Choi, S. W., Jia, J., Lazarou, M., Eskelinen, E., Johansen, T., & Deretic, V. P. (2019) · The EMBO Journal · doi:10.15252/embj.2019101994 · Cited by 63
“Human cells have 6 mAtg8s, with proposed but not fully delineated specialized functions (Shpilka et al, 2011).”
BackgroundHuynh, T. Y. L., Zaręba, I., Baszanowska, W., Lewoniewska, S., & Palka, J. A. (2020) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-020-03685-y · Cited by 59
Clinical Applications of Autophagy Proteins in Cancer: From Potential Targets to Biomarkers
Bortnik, S. B., & Gorski, S. M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071496 · Cited by 60
“Each family ember, while demonstrating some functional redundancy with other members, plays distinct roles in the autophagy process [35,43].”
BackgroundModulation of plant autophagy during pathogen attack
Leary, A. Y., Sanguankiattichai, N., Duggan, C., Tümtaş, Y., Pandey, P., Segretin, M. E., Linares, J. S., Savage, Z., Yow, R. J., & Bozkurt, T. O. (2017) · Journal of Experimental Botany · doi:10.1093/jxb/erx425 · Cited by 58
“138 ATG8 appears to have gone through a series of duplication events and diversified to encode 139 different isoforms in higher eukaryotes (Shpilka et al., 2011).”
BackgroundHuber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N. Y., Güntert, P., Đikić, I., Kirkin, V., Komatsu, M., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1606637 · Cited by 54
“This conformation flexibility for GABARAPs N-terminal regions was reported previously [43] and is important for interactions of Atg8-family proteins with proteins in and outside of autophagy pathways (reviewed in [9]).”
BackgroundRahman, M. A., Rahman, M. H., Hossain, M. S., Biswas, P., Islam, R., Uddin, M. J., Rahman, M. H., & Rhim, H. (2020) · Biomedicines · doi:10.3390/biomedicines8110517 · Cited by 58
“Microtubule-associated protein 1 light chain 3-beta (MAP1LC3B) and Atg5-Atg12 complex pathways, which are ubiquitin-like pathways, are regulatory for vesicle elongation and are encoded by the yeast Atg8 pathway, which has a human homologue [18].”
BackgroundDegradation of Organelles or Specific Organelle Components via Selective Autophagy in Plant Cells
Michaeli, S., & Galili, G. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15057624 · Cited by 56
“Among these proteins, ATG8 is one of the central best-studied proteins of the core autophagy machinery [11,36].”
BackgroundRodriguez, M., Kaushik, A. K., Lapierre, J., Dever, S. M., El‐Hage, N., & Nair, M. (2016) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-016-9688-3 · Cited by 56
“The genes for GABARAP and GABARAPL1 are subfamilies of MAP1LC3 and homologues of Atg8, which are all involved in elongation of the phagophore and formation of autophagosomes; however, the GABARAP subfamily is essential for a later stage of autophagosome maturation (Shpilka et al. 2011).”
BackgroundComplex Relations Between Phospholipids, Autophagy, and Neutral Lipids
Shatz, O., Holland, P., Elazar, Z., & Simonsen, A. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.08.001 · Cited by 57
“While yeast only have one Atg8 protein, seven mammalian Atg8 genes have been identified, belonging to the LC3 (LC3A, -B, -B2 and -C) or GABARAP [GABARAP, -L1, -L2 (also referred to as GATE-16)] subfamilies [146].”
BackgroundFormaldehyde exposure induces autophagy in testicular tissues of adult male rats
Han, S., Zhou, D.-X., Lin, P., Qin, Z., An, L., Zheng, L.-R., & Li, L. (2013) · Environmental Toxicology · doi:10.1002/tox.21910 · Cited by 54
“At present, genetic studies in yeast have identified 34 autophagy-related genes (Atg) that are required for initiation and performance of autophagy (Shpilka et al., 2011).”
BackgroundKyöstilä, K., Syrjä, P., Jagannathan, V., Chandrasekar, G., Jokinen, T. S., Seppälä, E. H., Becker, D., Drögemüller, M., Dietschi, E., Drögemüller, C., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005169 · Cited by 53
“Similar to the ATG4 proteins, mammals possess several homologs of the yeast Atg8 [27].”
BackgroundInfluentialAn inter‐species protein–protein interaction network across vast evolutionary distance
Zhong, Q., Pevzner, S. J., Hao, T., Wang, Y., Mosca, R., Menche, J., Taipale, M., Taşan, M., Fan, C., Yang, X., et al. (2016) · Molecular Systems Biology · doi:10.15252/msb.20156484 · Cited by 54
“Autophagy is a conserved eukaryotic pathway for sequestering and transporting cytoplasmic and organellar proteins to the lysosome for degradation (Shpilka et al, 2011).”
The interplay between autophagy and cGAS-STING signaling and its implications for cancer
Schmid, M., Fischer, P., Engl, M., Widder, J., Gruber, S., & Slade, D. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1356369 · Cited by 61
Selective Autophagy Receptors in Antiviral Defense
Viret, C., Duclaux‐Loras, R., Nancey, S., Rozières, A., & Faure, M. (2021) · Trends in Microbiology · doi:10.1016/j.tim.2021.02.006 · Cited by 50
Vps13D functions in a Pink1-dependent and Parkin-independent mitophagy pathway
Shen, J. L., Fortier, T. M., Wang, R., & Baehrecke, E. H. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202104073 · Cited by 47
“The Atg5/12/16 complex is required for lipidation of Atg8a and recruitment to the forming autophagosome (Shpilka et al., 2011).”
BackgroundDmon1 controls recruitment of Rab7 to maturing endosomes in Drosophila
Yousefian, J. F., Troost, T., Grawe, F., Sasamura, T., Fortini, M., & Klein, T. (2013) · Journal of Cell Science · doi:10.1242/jcs.114934 · Cited by 50
“ATG8 is a specific marker of the autophagosomal membrane in all stages of maturation (Shpilka et al., 2011).”
BackgroundPimentel, J. M., Zhou, J. Y., & Wu, G. S. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.217285 · Cited by 55
Li, Y., Cheng, X., Li, M., Wang, Y., Fu, T., Zhou, Z., Wang, Y., Gong, X., Xu, X., Liu, J., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2006997117 · Cited by 47
Ubiquitin-like proteins and autophagy at a glance
Shpilka, T., Mizushima, N., & Elazar, Z. (2012) · Journal of Cell Science · doi:10.1242/jcs.093757 · Cited by 53
“…genes encoding Atg8-like proteins that are divided into three subfamilies: microtubule-associated protein 1 light chain 3 (LC3), c-aminobutyric acid (GABA) receptor-associated protein (GABARAP) and Golgi-associated ATPase enhancer of 16 kDa (GATE16, also known as GABARAPL2) (Shpilka et al., 2011).”
BackgroundZhang, S., Hama, Y., & Mizushima, N. (2021) · Journal of Cell Science · doi:10.1242/jcs.233742 · Cited by 47
Zhang, M., Zhang, J., Lu, L., Qiu, Z.-Y., Zhang, X., Yu, S.-B., Wu, Y., & Wang, M.-Q. (2013) · Apoptosis · doi:10.1007/s10495-013-0811-0 · Cited by 46
“LC3, which is involved in the protein conjugation system, is required in the expansion of the autophagosome [17].”
Autophagy and checkpoints for intracellular pathogen defense
Paulus, G. L. C., & Xavier, R. J. (2014) · Current Opinion in Gastroenterology · doi:10.1097/mog.0000000000000134 · Cited by 53
Han, K., Jia, N., Zhong, Y., & Shang, X. (2017) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26452 · Cited by 47
“These results suggest that in APP/PS1 transgenic mice, autophagy is disrupted, such as blockage of autophagy initiation, low activity of autolysosome, and accumulation of autophagosome.(21) HNG treatment could induce ULK1 expression and increase ULK1 activity in the brain to promote autophagy in APP/PS1 transgenic mic…”
BackgroundAutophagy-related Proteins as a Prognostic Factor of Patients With Colorectal Cancer
Koustas, E., Sarantis, P., Theoharis, S., Saetta, A. A., Chatziandreou, I., Kyriakopoulou, G., Giannopoulou, I., Michelli, M., Schizas, D., Papavassiliou, A. G., et al. (2019) · American Journal of Clinical Oncology · doi:10.1097/coc.0000000000000592 · Cited by 44
Role of autophagy in cisplatin-induced ototoxicity
Youn, C. K., Kim, J., Park, J., Do, N., & Cho, S. I. (2015) · International Journal of Pediatric Otorhinolaryngology · doi:10.1016/j.ijporl.2015.08.012 · Cited by 47
Döring, T., & Prange, R. (2014) · Cellular Microbiology · doi:10.1111/cmi.12398 · Cited by 47
“…of more than 20 specific autophagy (Atg) proteins that mediate the formation and elongation of a doublemembrane sack (the isolation membrane), cargo engulfment, autophagophore closure and autophagosome fusion with the lysosome (Geng and Klionsky, 2008; Shpilka et al., 2011; Weidberg et al., 2011).”
BackgroundInfluentialThe Influence of Tumor Microenvironment on ATG4D Gene Expression in Colorectal Cancer Patients
Gil, J., Ramsey, D., Pawłowski, P., Szmida, E., Leszczyński, P., Bębenek, M., & Sasiadek, M. M. (2018) · Medical Oncology · doi:10.1007/s12032-018-1220-6 · Cited by 49
Gaviria, D. A., Paguio, M. F., Turnbull, L. B., Tan, A., Siriwardana, A., Ghosh, D., Ferdig, M. T., Sinai, A. P., & Roepe, P. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079059 · Cited by 45
“In all eukaryotic cell types examined, the re distribution of ATG8 protein to more widely disbursed puncta marks the induction of autophagy by starvation [46].”
BackgroundResultInfluentialLieberman, O. J., Cartocci, V., Pigulevskiy, I., Molinari, M., Carbonell, J., Broseta, M. B., Post, M. R., Sulzer, D., Borgkvist, A., & Santini, E. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00070 · Cited by 48
“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).”
BackgroundConjugation of ATG8s to single membranes at a glance
Figueras-Novoa, C., Timimi, L., Marcassa, E., Ulferts, R., & Beale, R. C. L. (2024) · Journal of Cell Science · doi:10.1242/jcs.261031 · Cited by 45
Echavarría-Consuegra, L., Smit, J. M., & Reggiori, F. (2019) · Open Biology · doi:10.1098/rsob.190009 · Cited by 46
Nuclear LC3 Associates with Slowly Diffusing Complexes that Survey the Nucleolus
Kraft, L. J., Manral, P., Dowler, J., & Kenworthy, A. K. (2016) · Traffic · doi:10.1111/tra.12372 · Cited by 44
“Microtubule-associated protein 1 light chain 3 (LC3), a ubiquitin-like protein that participates in autophagosome formation and autophagy cargo selection in the cytoplasm, is one of the most widely utilized markers of autophagy (1,2).”
BackgroundMethodChoi, S., & Kim, H. J. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.11.044 · Cited by 44
“1B), GATE16 (also known as GABARAPL2) is one of the seven mammalian homologs of the yeast ATG8 protein [9].”
BackgroundInfluentialDhingra, A., Bell, B. A., Peachey, N. S., Daniele, L. L., Reyes-Reveles, J., Sharp, R. C., Jun, B., Bazan, N. G., Sparrow, J. R., Kim, H. J., et al. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00351 · Cited by 41
“…LC3 isoforms were predicted to be functionally redundant, some studies suggest isoform specificity in selective Frontiers in Cellular Neuroscience | www.frontiersin.org 2 October 2018 | Volume 12 | Article 351 autophagy (Shpilka et al., 2011; Maruyama et al., 2014; Koukourakis et al., 2015).”
Interactions between Autophagy and DNA Viruses
Yin, H., Shao, S., Jiang, X.-J., Xie, P.-Y., Sun, W.-S., & Yu, T. (2019) · Viruses · doi:10.3390/v11090776 · Cited by 44
Post-Translational Modifications of ATG4B in the Regulation of Autophagy
Park, N. Y., Jo, D. S., & Cho, D. (2022) · Cells · doi:10.3390/cells11081330 · Cited by 43
“ATG8 plays an essential role in autophagosome formation and phagophore elongation [7].”
BackgroundUbiquitin-like proteins and their roles in archaea
Maupin-furlow, J. A. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2012.09.006 · Cited by 42
Aveic, S., & Tonini, G. P. (2016) · Cancer Cell International · doi:10.1186/s12935-016-0341-2 · Cited by 44
“Then, the processing of microtubule-associated protein 1 light chain 3 (LC3), a well-accepted hallmark of autophagosomes, starts with cleavage in the cytosol (LC3-I) and lipidation (LC3-II) [17, 18], guiding the autophagosome toward an autophagolysosome.”
BackgroundNagel, B. M., Bechtold, M., Rodriguez, L. G., & Bogdan, S. (2017) · Journal of Cell Science · doi:10.1242/jcs.193086 · Cited by 43
“In flies, Atg6 is also required for multiple vesicle trafficking pathways and hematopoiesis (Shravage et al., 2013).”
BackgroundRather, R. A., Bhagat, M., & Singh, S. K. (2020) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2020.108321 · Cited by 43
RNA and Protein Delivery by Cell‐Secreted and Bioengineered Extracellular Vesicles
Wang, B. Z., Luo, L. J., & Vunjak‐Novakovic, G. (2021) · Advanced Healthcare Materials · doi:10.1002/adhm.202101557 · Cited by 45
Functional Amino Acids and Autophagy: Diverse Signal Transduction and Application
Liu, C., Ji, L., Hu, J., Zhao, Y., Johnston, L. J., Zhang, X., & Ma, X. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111427 · Cited by 44
“Overall, the molecular mechanism of the autophagy process is carried out by autophagy-related genes (Atgs) and several critical complexes (Figure 1) [11].”
BackgroundAvoidance and Subversion of Eukaryotic Homeostatic Autophagy Mechanisms by Bacterial Pathogens
Miller, C. N., & Celli, J. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.07.007 · Cited by 42
“A uthor M anuscript A uthor M anuscript A uthor M anuscript A uthor M anuscript ER endoplasmic reticulum ERAD endoplasmic reticulum-associated degradation ERES endoplasmic reticulum exit sites FPI Francisella pathogenicity island GABARAP γ-aminobutyric acid receptor-associated protein GATE-16 Golgi-associated ATPase e…”
BackgroundGuerrero‐Gómez, D., Mora-Lorca, J. A., Sáenz‐Narciso, B., Naranjo-Galindo, F. J., Muñoz-Lobato, F., Parrado‐Fernández, C., Goikolea, J., Cedazo-Mı́nguez, Á., Link, C. D., Néri, C., et al. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-018-0270-9 · Cited by 44
Contribution of autophagy to antiviral immunity
Rey-Jurado, E., Riedel, C. A., González, P. A., Bueno, S. M., & Kalergis, A. M. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.07.047 · Cited by 40
“Gamma-aminobutyric acid receptor-associated protein (GABARAP) and Golgi-associated ATPase enhancer of 16kDa (GATE-16) are homologs of LC3 and are involved in the late stages of autophagosome maturation [33].”
BackgroundHan, D., Wan, C., Liu, F., Xu, X., Jiang, L., & Xu, J. (2016) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2016/9593716 · Cited by 40
Autophagy as a Homeostatic Mechanism in Response to Stress Conditions in the Central Nervous System
Gerónimo‐Olvera, C., & Massieu, L. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1546-x · Cited by 39
The twoC. elegansATG-16 homologs have partially redundant functions in the basal autophagy pathway
Zhang, H., Wu, F., Wang, X., Du, H., Wang, X., & Zhang, H. (2013) · Autophagy · doi:10.4161/auto.26095 · Cited by 39
Here, There Be Dragons : Charting Autophagy-Related Alterations in Human Tumors
Lebovitz, C. B., Bortnik, S. B., & Gorski, S. M. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-2465 · Cited by 40
“In addition, GABARAP/GATE-16 members function in intracellular protein trafficking (94).”
BackgroundDecrease of autophagy activity promotes malignant progression of tongue squamous cell carcinoma
Wang, Y., Wang, C., Tang, H., Wang, M., Weng, J., Liu, X., Zhang, R., Huang, H., & Hou, J. (2013) · Journal of Oral Pathology and Medicine · doi:10.1111/jop.12049 · Cited by 39
Autophagy proteins are not universally required for phagosome maturation
Cemma, M., Grinstein, S., & Brumell, J. H. (2016) · Autophagy · doi:10.1080/15548627.2016.1191724 · Cited by 40
“LC3 is a ubiquitin-like molecule that is covalently conjugated to phosphatidylethanolamine on phagophore membranes through a series of reactions similar to ubiquitin conjugation and requires a subset of ATG proteins, including ATG5 and ATG7.”
BackgroundNew Visions on Natural Products and Cancer Therapy: Autophagy and Related Regulatory Pathways
Martelli, A., Omrani, M., Zarghooni, M., Citi, V., Brogi, S., Calderone, V., Sureda, A., Lorzadeh, S., Rosa, S. C. D. S., Grabarek, B. O., et al. (2022) · Cancers · doi:10.3390/cancers14235839 · Cited by 40
Autophagy: A Key Player in Pancreatic Cancer Progression and a Potential Drug Target
Gillson, J., El-Aziz, Y. S. A., Leck, L. Y. W., Jansson, P. J., Pavlakis, N., Samra, J. S., Mittal, A., & Sahni, S. (2022) · Cancers · doi:10.3390/cancers14143528 · Cited by 38
Ryabovol, V., & Minibayeva, F. V. (2016) · Biochemistry (Moscow) · doi:10.1134/s0006297916040052 · Cited by 37
“The ubiquitin domain in ATG8 proteins is mostly conserved among the members of the family and might play an important role in pro tein–ligand interactions [79].”
BackgroundInfluentialCackovic, J., Gutierrez-Luke, S., Call, G. B., Juba, A. N., O’Brien, S., Jun, C. H., & Buhlman, L. M. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00039 · Cited by 40
RETRACTED: Trehalose restores functional autophagy suppressed by high glucose
Xu, C., Chen, X., Sheng, W.-B., & Yang, P. (2019) · Reproductive Toxicology · doi:10.1016/j.reprotox.2019.02.005 · Cited by 37
“Nutritional deficiency induces autophagy by activating the Atg1 complex and inhibiting the mammalian target of rapamycin (mTOR) [13] or by activating the Beclin1/PI3KCIII/ Ambra1 complex [14,15].”
BackgroundRetractedThe Interplay of HIV and Autophagy in Early Infection
Cabrera-Rodríguez, R., Pérez-Yanes, S., Estévez‐Herrera, J., Márquez-Arce, D., Cabrera, C., Espert, L., Blanco, J., & Valenzuela-Fernández, A. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.661446 · Cited by 37
Wu, J., Guo, J., Cao, Q., Wáng, Y., Chen, J., Wang, Z., & Yuan, Z. (2016) · Oncology Letters · doi:10.3892/ol.2016.5476 · Cited by 37
“LC3 is a specific marker of autophagosomes in mammalian cells, and the conversion of the soluble form of LC3 (LC3-I) to the autophagosome-associated form (LC3-II) is a characteristic of autophagy (33-35).”
LC3B is lipidated to large lipid droplets during prolonged starvation for noncanonical autophagy
Omrane, M., M’Barek, K. B., Santinho, A., Nguyen, N., Nag, S., Melia, T. J., & Thiam, A. R. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.05.009 · Cited by 37
Phospholipids in Autophagosome Formation and Fusion
Martens, S., Nakamura, S., & Yoshimori, T. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.10.029 · Cited by 37
“In yeast there is one Atg8 protein while there are several ATG8 isoforms in mammalian cells, which are subdivided into the LC3s and GABARAPs [46].”
BackgroundLegionella RavZ Plays a Role in Preventing Ubiquitin Recruitment to Bacteria-Containing Vacuoles
Kubori, T., Bui, X. T., Hubber, A. M., & Nagai, H. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00384 · Cited by 38
“Atg8 is a yeast counterpart of LC3, and structural studies of Atg8 family proteins including LC3 (Kouno et al., 2005) revealed structural similarity to ubiquitin (Shpilka et al., 2011).”
BackgroundZhang, J., Qu, Z., Yao, H. W., Sun, L., Harata‐Lee, Y., Cui, J., Aung, T. N., Liu, X., You, R., Wang, W., et al. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109169 · Cited by 34
Song, L., Yao, L., Zhang, L., Piao, Z., & Lu, Y. (2020) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-019-01792-2 · Cited by 36
Li, J., Breker, M., Graham, M. M., Schuldiner, M., & Hochstrasser, M. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008387 · Cited by 35
“Loss of ATG8 eliminates all types of macroautophagy [45], while ATG11 and ATG39 are needed for specific classes of selective macroautophagy [18].”
BackgroundRodriguez, A. E., López‐Crisosto, C., Peña‐Oyarzún, D., Salas, D., Parra, V., Quiroga, C., Morawe, T., Chiong, M., Behl, C., & Lavandero, S. (2015) · Autophagy · doi:10.1080/15548627.2015.1124225 · Cited by 34
“MAP1LC3B/LC3B (microtubule-associated protein 1 light chain 3 b) is an ortholog of yeast Atg8, that in mammalian cells includes MAP1LC3 (MAP1LC3A, MAP1LC3B, and MAP1LC3C), GABARAP (GABA[A] receptor-associated protein), GABARAPL1 (GABA[A] receptor-associated protein like 1) and GABARAPL2/ GATE-16 (GABA[A] receptor-asso…”
BackgroundExpanding the view of the molecular mechanisms of autophagy pathway
Majeed, S. T., Majeed, R., & Andrabi, K. I. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30819 · Cited by 36
“ATG8 family proteins belong to two subgroups: the LC3 (light chain 3) subfamily that includes LC3A, LC3B, LC3B2, LC3C, and the g‐aminobutyric acid receptor‐associated protein (GABARAP) subfamily that includes GABARAP, GABAR- APL1 and GABARAPL2 (Kabeya et al., 2004; Shpilka et al., 2011).”
BackgroundATI1, a newly identified atg8-interacting protein, binds two different Atg8 homologs
Avin‐Wittenberg, T., Michaeli, S., Honig, A., & Galili, G. (2012) · Plant Signaling & Behavior · doi:10.4161/psb.20030 · Cited by 34
Shafik, N. M., El‐Esawy, R. O., Mohamed, D. A., Deghidy, E. A., & El‐Deeb, O. S. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.108095 · Cited by 33
Structure and Dynamics in the ATG8 Family From Experimental to Computational Techniques
Sora, V., Kumar, M., Maiani, E., Lambrughi, M., Tiberti, M., & Papaleo, E. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00420 · Cited by 33
“ATG8 proteins are highly conserved in eukaryotes (King, 2012) and exist in the form of one or several orthologs (Shpilka et al., 2011).”
BackgroundDiscovery and optimization of pyrazolopyrimidine sulfamates as ATG7 inhibitors
Huang, S., Adhikari, S., Brownell, J. E., Calderwood, E. F., Chouitar, J., D’Amore, N. R., England, D. B., Foley, K., Harrison, S. J., Leroy, P. J., et al. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2020.115681 · Cited by 32
Autophagy Requirements for Eye Lens Differentiation and Transparency
Brennan, L., Costello, M. J., Hejtmancik, J. F., Menko, A. S., Riazuddin, S., Shiels, A., & Kantorow, M. (2023) · Cells · doi:10.3390/cells12030475 · Cited by 33
“The ATG8 family proteins are divided into two subgroups: the LC3 (light chain 3) subfamily, which includes LC3A, LC3B, LC3B2, and LC3C, and the g-aminobutyric acid receptor-associated protein (GABARAP) subfamily, which includes GABARAP, GABARAPL1, and GABARAPL2 [25,26,31,32].”
BackgroundZhu, Y., Zhang, M., Kelly, A. R., & Cheng, A. (2014) · Bioscience Reports · doi:10.1042/bsr20140053 · Cited by 33
Size, stoichiometry, and organization of soluble LC3-associated complexes
Kraft, L. J., Nguyen, T. A., Vogel, S. S., & Kenworthy, A. K. (2014) · Autophagy · doi:10.4161/auto.28175 · Cited by 31
“ATG8 proteins share high structural (but not sequence) homology with ubiquitin, and thus have been termed ubiquitin-like proteins.(12) Interestingly, unlike ubiquitin, which is conjugated to other proteins, ATG8 proteins are conjugated to the head group of the lipid phosphatidylethanolamine.”
BackgroundInhibition of the mTOR Pathway Exerts Cardioprotective Effects Partly through Autophagy in CLP Rats
Han, W., Wang, H., Su, L., Long, Y., Cui, N., & Liu, D. (2018) · Mediators of Inflammation · doi:10.1155/2018/4798209 · Cited by 32
Autophagosomal Protein Dynamics and Influenza Virus Infection
Dumit, V. I., & Dengjel, J. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00043 · Cited by 31
“The binding is mediated by the 22 amino acid-residue sequence forming the conserved LIR motif with the core W/YxxL/I, which is indispensable for LC3 recruitment into p62-positive inclusion bodies (Figures 4B,C; Pankiv et al., 2007; Shpilka et al., 2011).”
BackgroundÁvila, L., Marmagne, A., Soulay, F., & Masclaux‐Daubresse, C. (2016) · Agronomy · doi:10.3390/agronomy6010015 · Cited by 36
“The presence of several different HvATG8 and HvATG18 genes in the barley genome—as also observed in other plants and animals, but not in yeast—suggests that autophagic machinery has adapted to environmental and developmental changes by duplicating these ATG genes [47], thereby providing several protein isoforms coded…”
BackgroundZhai, Y., Wang, H., Liang, M., & Lu, M. (2017) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2017.06.009 · Cited by 32
Role of Mitochondria–ER Contact Sites in Mitophagy
Rühmkorf, A., & Harbauer, A. B. (2023) · Biomolecules · doi:10.3390/biom13081198 · Cited by 35
“The Atg8-positive membranes will enable the formation of the double-layered autophagosomes [42] and engulf cargo targeted by autophagy adaptors.”
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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