How to Interpret LC3 Immunoblotting
Open accessAbstract
Microtubule-associated protein light chain 3 (LC3) is now widely used to monitor autophagy. One approach is to detect LC3 conversion (LC3-I to LC3-II) by immunoblot analysis because the amount of LC3-II is clearly correlated with the number of autophagosomes. However, LC3-II itself is degraded by autophagy, making interpretation of the results of LC3 immunoblotting problematic. Furthermore, the amount of LC3 at a certain time point does not indicate autophagic flux, and therefore, it is important to measure the amount of LC3-II delivered to lysosomes by comparing LC3-II levels in the presence and absence of lysosomal protease inhibitors. Another problem with this method is that LC3-II tends to be much more sensitive to be detected by immunoblotting than LC3-I. Accordingly, simple comparison of LC3-I and LC3-II, or summation of LC3-I and LC3-II for ratio determinations, may not be appropriate, and rather, the amount of LC3-II can be compared between samples.
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LC3 is required for autophagosome formation.
“LC3, which is a post-translational modifier, is required for autophagosome formation (Mizushima and Yoshimori, 2007).”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Mizushima and Yoshimori, 2007
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“LC3-II localizes to autophagosomes that ultimately fuse with lysosomes (autolysosomes) and is consequently degraded by lysosomal hydrolases [58,59].”
BackgroundAMPK–SKP2–CARM1 signalling cascade in transcriptional regulation of autophagy
Shin, H. R., Kim, H.-K., Oh, S., Lee, J.-G., Kee, M., Ko, H., Kweon, M., Won, K., & Baek, S. H. (2016) · Nature · doi:10.1038/nature18014 · Cited by 441 · see citing works
Molecular machinery and interplay of apoptosis and autophagy in coronary heart disease
Dong, Y., Chen, H., Gao, J., Liu, Y., Li, J., & Wang, J. (2019) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2019.09.001 · Cited by 442 · see citing works
ER stress negatively regulates AKT/TSC/mTOR pathway to enhance autophagy
Qin, L., Wang, Z., Tao, L., & Wang, Y. (2010) · Autophagy · doi:10.4161/auto.6.2.11062 · Cited by 435 · see citing works
Yang, D.-S., Stavrides, P., Mohan, P. S., Kaushik, S., Kumar, A., Ohno, M., Schmidt, S. D., Wesson, D., Bandyopadhyay, U., Jiang, Y., et al. (2011) · Brain · doi:10.1093/brain/awq341 · Cited by 429 · see citing works
Autophagy promotes the survival of dormant breast cancer cells and metastatic tumour recurrence
Ramírez, L. V., Vodnala, S. K., Nini, R., Hunter, K. W., & Green, J. E. (2018) · Nature Communications · doi:10.1038/s41467-018-04070-6 · Cited by 433 · see citing works
PGC-1α-mediated regulation of mitochondrial function and physiological implications
Halling, J. F., & Pilegaard, H. (2020) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2020-0005 · Cited by 418 · see citing works
“In addition, lipidation of light chain (LC)3I to LC3II is required for autophagosome maturation (Mizushima & Komatsu, 2011), which is why the content of LC3II and the ratio of LC3II/LC3I are often used as markers of autophagy activation (Kabeya et al., 2000;Mizushima & Yoshimori, 2007).”
BackgroundAutophagy in microglia degrades extracellular β-amyloid fibrils and regulates the NLRP3 inflammasome
Cho, M.-H., Cho, K., Kang, H.-J., Jeon, E.-Y., Kim, H.-S., Kwon, H.-J., Kim, H.-M., Kim, D.-H., & Yoon, S.-Y. (2014) · Autophagy · doi:10.4161/auto.29647 · Cited by 395 · see citing works
“bBraak stage based on neurofibrillary tangles was 5 or 6 in aD cases, and 0 or 1 in controls.(25) cBraak stage based on amyloid plaques was c in aD cases, and 0 or a in controls.”
BackgroundChloroquine sensitizes breast cancer cells to chemotherapy independent of autophagy
Maycotte, P., Aryal, S., Cummings, C. T., Thorburn, J., Morgan, M. J., & Thorburn, A. M. (2012) · Autophagy · doi:10.4161/auto.8.2.18554 · Cited by 401 · see citing works
“However, LC3II is also degraded inside the lysosomes or de-conjugated by Atg4.(4,24) Therefore, in order to measure autophagic flux, lysosomal inhibitors (CQ, Baf A, pepstatin A/E64D) are used in order to inhibit LC3II degradation, since in the absence of these inhibitors, an autophagy-inducing treatment can result in…”
BackgroundA role for autophagy during hepatic stellate cell activation
Thoen, L. F. R., Guimarães, E. L. M., Dollé, L., Mannaerts, I., Najimi, M., Sokal, E., & van Grunsven, L. A. (2011) · Journal of Hepatology · doi:10.1016/j.jhep.2011.07.010 · Cited by 385 · see citing works
“We first investigated the expression of LC3B, a protein involved in autophagosome formation [14], in total liver samples of healthy and 4 week CCl4-treated mice (Fig.”
BackgroundTanaka, S., Hikita, H., Tatsumi, T., Sakamori, R., Nozaki, Y., Sakane, S., Shiode, Y., Nakabori, T., Saito, Y., Hiramatsu, N., et al. (2016) · Hepatology · doi:10.1002/hep.28820 · Cited by 376 · see citing works
“To confirm this hypothesis, we compared LC3-II expression levels in the presence and absence of bafilomycin, which inhibits lysosomal enzyme activity as well as the fusion of autophagosomes with lysosomes.((23)) Bafilomycin clearly increased levels of LC3-II expression in control HepG2 cells.”
BackgroundMethodSelf-citationLoss of the Parkinson's disease-linked gene DJ-1 perturbs mitochondrial dynamics
Irrcher, I., Aleyasin, H., Seifert, E. L., Hewitt, S. J., Chhabra, S., Phillips, M., Lutz, A. K., Rousseaux, M. W. C., Bevilacqua, L., Jahani‐Asl, A., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq288 · Cited by 386 · see citing works
Jiang, M., Liu, K., Luo, J., & Dong, Z. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090594 · Cited by 375 · see citing works
Ebrahimi‐Fakhari, D., Cantuti‐Castelvetri, I., Fan, Z., Rockenstein, E. M., Masliah, E., Hyman, B. T., McLean, P. J., & Unni, V. K. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.1560-11.2011 · Cited by 378 · see citing works
“7A,B), indicating an accumulation of autophagosomes consistent with a block in autophagic clearance by BafA1 (Mizushima and Yoshimori, 2007; Klionsky et al., 2008; Mizushima et al., 2010).”
BackgroundKrebiehl, G., Ruckerbauer, S., Burbulla, L. F., Kieper, N., Maurer, B., Waak, J., Wolburg, H., Gizatullina, Z. Z., Gellerich, F. N., Woitalla, D., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009367 · Cited by 370 · see citing works
“In contrast, the usage of GFP-WIPI-1 does not lead to such protein aggregations [25].”
BackgroundMethodSahani, M. H., Itakura, E., & Mizushima, N. (2014) · Autophagy · doi:10.4161/auto.27344 · Cited by 363 · see citing works
“1A).(8,20,21) LC3 conversion from LC3-I to LC3-II and inhibition of MTORC1 (dephosphorylation of RPS6KB/p70 S6 kinase and EIF4EBP1/4E-BP1) were simultaneously observed.”
Self-citationYang, B., Ding, L. S., Yao, H., Chen, Y., & Shi, J. (2020) · Advanced Materials · doi:10.1002/adma.201907152 · Cited by 364 · see citing works
Dysfunctional autophagy in RPE, a contributing factor in age-related macular degeneration
Golestaneh, N., Chu, Y., Xiao, Y.-Y., Stoleru, G. L., & Theos, A. C. (2017) · Cell Death & Disease · doi:10.1038/cddis.2016.453 · Cited by 357 · see citing works
“after lipidation becomes LC3-II, is inserted into the inner and outer membranes of the AP and is eventually degraded.(34)”
A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin
Sarkar, S., Krishna, G., Imarisio, S., Saiki, S., O’Kane, C. J., & Rubinsztein, D. C. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm294 · Cited by 348 · see citing works
Zhu, K., Dunner, K., & McConkey, D. J. (2010) · Oncogene · doi:10.1038/onc.2009.343 · Cited by 338 · see citing works
“Accumulation of LC3II in the presence of lysosomal protease inhibitors is indicative of enhancement of autophagic flux (Mizushima and Yoshimori, 2007).”
BackgroundAutophagy is cytoprotective during cisplatin injury of renal proximal tubular cells
Periyasamy‐Thandavan, S., Jiang, M., Wei, Q., Smith, R., Yin, X., & Dong, Z. (2008) · Kidney International · doi:10.1038/ki.2008.214 · Cited by 319 · see citing works
“Together, these results have demonstrated evidence for the occurrence of autophagy during cisplatin-induced renal cell injury.”
BackgroundA Non-canonical MEK/ERK Signaling Pathway Regulates Autophagy via Regulating Beclin 1
Wang, J., Whiteman, M. W., Lian, H., Wang, G., Singh, A. K., Huang, D., & Denmark, T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.026013 · Cited by 319 · see citing works
Defining and measuring autophagosome flux—concept and reality
Loos, B., du Toit, A., & Hofmeyr, J. S. (2014) · Autophagy · doi:10.4161/15548627.2014.973338 · Cited by 317 · see citing works
“Immunoblotting for endogenous LC3 is one of the crucial functional reporter assays that can be used to reliably monitor autophagosome synthesis or degradation, as LC3 associates with the lumenal and cytosolic surface of autophagosomes, with a degree of recycling taking place from the cytosolic surface.(9) However, wes…”
BackgroundKim, R. H., Coates, J. M., Bowles, T. L., McNerney, G. P., Sutcliffe-Goulden, J., Jung, J. U., Gandour‐Edwards, R. F., Chuang, F. Y. S., Bold, R. J., & Kung, H.-J. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-3157 · Cited by 316 · see citing works
“Increase in total autophagic flux was confirmed with chloroquine (30), an autophagy inhibitor that disrupts lysosomal function”
BackgroundWhy should autophagic flux be assessed?
Zhang, X.-J., Chen, S., Huang, K.-X., & Le, W.-D. (2013) · Acta Pharmacologica Sinica · doi:10.1038/aps.2012.184 · Cited by 308 · see citing works
Autophagy in ovary and polycystic ovary syndrome: role, dispute and future perspective
Kumariya, S., Ubba, V., Jha, R. K., & Gayen, J. R. (2021) · Autophagy · doi:10.1080/15548627.2021.1938914 · Cited by 306 · see citing works
Proline Metabolism and Microenvironmental Stress
Phang, J. M., Liu, W., & Zabirnyk, O. (2010) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.012809.104638 · Cited by 303 · see citing works
“By contrast, the oxLDL induction of the conversion of LC3-I to LC3-II, hallmarks for the onset of autophagy (77), was markedly decreased by POX knockdown.”
Thyroid hormone stimulates hepatic lipid catabolism via activation of autophagy
Sinha, R. A., You, S.-H., Zhou, J., Siddique, M. M., Bay, B.-H., Zhu, X., Privalsky, M. L., Cheng, S.-Y., Stevens, R. D., Summers, S. A., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci60580 · Cited by 303 · see citing works
Rodríguez-Navarro, J. A., Rodríguez, L., Casarejos, M. J., Solano, R. M., Gómez, A., Perucho, J., Cuervo, A. M., García de Yébenes, J., & Mena, M. A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.014 · Cited by 298 · see citing works
“However, LC3 II/LC3 I as well as LC3 II/β-actin ratio (Mizushima and Yoshimori, 2007), was increased after 2.”
InfluentialHigh-Mobility Group Box 1 Is Essential for Mitochondrial Quality Control
Tang, D., Kang, R., Livesey, K. M., Kroemer, G., Billiar, T. R., Houten, B. V., Zeh, H. J., & Lotze, M. T. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.04.008 · Cited by 296 · see citing works
“, 2005), or blocking lysosomal degradation by pepstatin and E64D (lysosomal protease inhibitors) (Mizushima and Yoshimori, 2007) increased rotenone-mediated”
Li, L., Chen, Y., & Gibson, S. B. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.09.020 · Cited by 292 · see citing works
The inositol 1,4,5-trisphosphate receptor regulates autophagy through its interaction with Beclin 1
Vicencio, J. M., Ortiz, C., Criollo, A., Jones, A. W. E., Kepp, O., Galluzzi, L., Joza, N., Vitale, I., Morselli, E., Tailler, M., et al. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2009.34 · Cited by 289 · see citing works
“The redistribution of GFP-LC3 to dots or the accumulation of LC3-II may be a sign of an enhanced formation of autophagosomes or a reduced removal of autophagosomes.(33,34) To discriminate between these two possibilities, we blocked the fusion between autophagosomes and lysosomes (with bafilomycin A1) and/or inhibited…”
Campbell, G. R., & Spector, S. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002689 · Cited by 282 · see citing works
“The accumulation of LC3B-II was increased in the presence of the lysosomal protease inhibitor pepstatin A regardless of infection status (Figure 2B), indicative of autophagic flux [33].”
BackgroundKiyono, K., Suzuki, H. I., Matsuyama, H., Morishita, Y., Komuro, A., Kano, M. R., Sugimoto, K., & Miyazono, K. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4401 · Cited by 285 · see citing works
“We next determined the autophagy flux by LC3 turnover assay, which measures the amount of LC3-II delivered to the lysosomes by comparing the LC3-II amounts in the presence and absence of lysosomal inhibitors (29, 30).”
Shehata, M., Matsumura, H., Okubo-Suzuki, R., Ohkawa, N., & Inokuchi, K. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.4533-11.2012 · Cited by 285 · see citing works
“Monitoring autophagic flux is recommended, because the increase in the LC3-II/LC3-I ratio may be attributable to either the induction of AP formation or the blockade of AP–lysosomal fusion (Mizushima and Yoshimori, 2007).”
BackgroundTranscription Factor GATA4 Inhibits Doxorubicin-induced Autophagy and Cardiomyocyte Death
Kobayashi, S., Volden, P. A., Timm, D. J., Mao, K., Xu, X., & Liang, Q. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.070037 · Cited by 285 · see citing works
Kang, R., Tang, D., Schapiro, N. E., Livesey, K. M., Farkas, A. M., Loughran, P., Bierhaus, A., Lotze, M. T., & Zeh, H. J. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.149 · Cited by 333 · see citing works
“method for detecting autophagy is measuring enhanced degradation of p62 (SQSTM1/sequestosome), a long-lived scaffolding protein involved in the transport of ubiquitinated proteins destined for proteosomal digestion.(22,23) Indeed, knockdown of RAGE limited degradation of p62 induced by chemotherapeutic agents (Figure…”
MethodChoi, K. S. (2012) · Experimental & Molecular Medicine · doi:10.3858/emm.2012.44.2.033 · Cited by 284 · see citing works
“…of the regulatory mechanisms governing the early steps of autophagy, including autophagosome formation (initiation, nucleation and elongation) (Mizushima and Yoshimori, 2007), those governing the later steps of autophagy, such as autophagosomal maturation and lysosomal degradation, are less…”
BackgroundInfluentialAntagonism of Beclin 1‐dependent autophagy by BCL‐2 at the endoplasmic reticulum requires NAF‐1
Chang, N. C., Nguyen, M., Germain, M., & Shore, G. C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.369 · Cited by 281 · see citing works
“Thus, cell lysates were analysed by immunoblot (Swerdlow et al, 2008) for conversion of the cytoplasmic form of microtubule-associated protein 1 light chain 3 (LC3 I form) to LC3 II, which is widely used to assay autophagosome accumulation (Mizushima and Yoshimori, 2007; Figure 3C).”
BackgroundMethodRole of JNK1-dependent Bcl-2 Phosphorylation in Ceramide-induced Macroautophagy
Pattingre, S., Bauvy, C., Carpentier, S., Levade, T., Levine, B., & Codogno, P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805920200 · Cited by 280 · see citing works
Cao, Y., Chen, J., Ren, G., Zhang, Y., Tan, X., & Yang, L. (2019) · Nutrients · doi:10.3390/nu11112794 · Cited by 281 · see citing works
“Therefore, it is critical to explore the amount of LC3II delivered to lysosomes by comparing LC3II and p62 levels with or without the lysosomal protease inhibitors, including chloroquine or bafilomycin A1 [17].”
BackgroundAutophagy regulates selective HMGB1 release in tumor cells that are destined to die
Thorburn, J., Horita, H., Redzic, J., Hansen, K., Frankel, A. E., & Thorburn, A. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2008.143 · Cited by 268 · see citing works
“Autophagic flux assays were performed by western blotting for LC3-II formation after treatment with DTEGF in the presence or absence of lysosomal protease inhibitors as recommended by Mizushima and Yoshimori (25), by monitoring the processing of a GST-tagged version of the autophagy cargo protein betaine homocysteine…”
MethodControl of autophagy initiation by phosphoinositide 3‐phosphatase jumpy
Vergne, I., Roberts, E., Elmaoued, R. A., Tosch, V., Delgado, M. A., Proikas‐Cezanne, T., Laporte, J., & Deretic, V. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.159 · Cited by 270 · see citing works
“To discern whether LC3-II increase following Jumpy or MTMR6 knock-downs was due to autophagy stimulation or inhibition of LC3-II degradation, Bafilomycin A1 (BafA1) and lysosomal protease inhibitors were added during the 30-min treatment (Mizushima and Yoshimori, 2007).”
Golgi-resident Small GTPase Rab33B Interacts with Atg16L and Modulates Autophagosome Formation
Itoh, T., Fujita, N., Kanno, E., Yamamoto, A., Yoshimori, T., & Fukuda, M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1231 · Cited by 271 · see citing works
“To determine whether the observed effect was caused by upregulation of autophagosome formation or blockage of autophagic degradation (Mizushima and Yoshimori, 2007), accumulation of LC3-II in the presence of H /K ionophore nigericin was investigated.”
BackgroundSelf-citationAutophagy is involved in influenza A virus replication
Zhou, Z., Jiang, X.-J., Liu, D., Fan, Z., Hu, X., Yan, J., Wang, M., & Gao, G. (2009) · Autophagy · doi:10.4161/auto.5.3.7406 · Cited by 269 · see citing works
Shimizu, S., Takehara, T., Hikita, H., Kodama, T., Tsunematsu, H., Miyagi, T., Hosui, A., Ishida, H., Tatsumi, T., Kanto, T., et al. (2011) · International Journal of Cancer · doi:10.1002/ijc.26374 · Cited by 266 · see citing works
“During the progress of autophagy, the cytoplasmic form LC3-I is converted to the membrane-bound lipidated form LC3-II which is detected by a mobility shift on electrophoresis.(15) When Huh7 cells were treated with 10 lM sorafenib, LC3 conversion was observed as early as 1 hr after the treatment and gradually increased…”
BackgroundSelf-citationAutophagy contributes to resistance of tumor cells to ionizing radiation
Chaachouay, H., Ohneseit, P., Toulany, M., Kehlbach, R., Multhoff, G., & Rodemann, H. P. (2011) · Radiotherapy and Oncology · doi:10.1016/j.radonc.2011.06.002 · Cited by 265 · see citing works
“of autophagosomes [16,17].”
Autophagosome Formation Depends on the Small GTPase Rab1 and Functional ER Exit Sites
Zoppino, F. C. M., Militello, R. D., Slavin, I., Álvarez, C., & Colombo, M. I. (2010) · Traffic · doi:10.1111/j.1600-0854.2010.01086.x · Cited by 263 · see citing works
“Therefore, autophagy can be monitored by the conversion of GFP-LC3-I to GFP-LC3-II, which can be detected by immunoblotting as LC3-II migrates faster than GFP-LC3-I during SDS–PAGE (42).”
BackgroundFilomeni, G., Graziani, I., Zio, D. D., Dini, L., Centonze, D., Rotilio, G., & Ciriolo, M. R. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.05.021 · Cited by 262 · see citing works
The Parkinson-associated protein PINK1 interacts with Beclin1 and promotes autophagy
Michiorri, S., Gelmetti, V, Giarda, E., Lombardi, F., Romano, F., Marongiu, R., Nerini-Molteni, S., Sale, P., Vago, R., Arena, G., et al. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.200 · Cited by 260 · see citing works
Kuo, T.-C., Chen, C., Baron, D. M., Önder, T. T., Loewer, S., Almeida, S., Weismann, C. M., Xu, P., Houghton, J., Gao, F., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2332 · Cited by 253 · see citing works
- Authors
- Mizushima, N., & Yoshimori, T.
- Affiliations
- Tokyo Medical and Dental University (JP)
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2007-11-26
- Volume
- 3
- Issue
- 6
- Pages
- 542-545
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- OpenAlex
- W1963521777
- Semantic Scholar
- ab5143ed104a787ff2e14d915df9a12ce5f5871a
- Cited by
- 2,595
- References
- 21
- Citations by year
- 2026: 62 · 2025: 114 · 2024: 152 · 2023: 141 · 2022: 176 · 2021: 164 · 2020: 173 · 2019: 155 · 2018: 177 · 2017: 162 · 2016: 167 · 2015: 179 · 2014: 137 · 2013: 165 · 2012: 120
- FWCI
- 52.76
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc
- Locations
- Autophagy (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- Kato Memorial Bioscience Foundation
- Toray Science Foundation
- Japan Society for the Promotion of Science
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- LC3, autophagic flux
- MeSH terms
- Animals, Autophagy, Humans, Lysosomes, Microtubule-Associated Proteins, Phosphatidylethanolamines, Sensitivity and Specificity, Immunoblotting, PC12 Cells, Cell Line, Tumor, Adaptor Proteins, Signal Transducing, Rats
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