The DOI matches its Crossref record; 20 of the 21 references it cites were found in a registry or an index.
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, 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
In the citing paper
“In neurons ATG9 localizes to axons and presynaptic sites, and requires active transport by the kinesin motor KIF1A to direct its localization into distal neurites [30,537].”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [30]
Citations
Cites
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
Self-citationBjørkøy, 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
The role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865
Self-citationThe role of autophagy in cardiomyocytes in the basal state and in response to hemodynamic stress
Nakai, A., Yamaguchi, O., Takeda, T., Higuchi, Y., Hikoso, S., Taniike, M., Omiya, S., Mizote, I., Matsumura, Y., Asahi, M., et al. (2007) · Nature Medicine · doi:10.1038/nm1574 · Cited by 1,520
Self-citationLC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation
Kabeya, Y., Mizushima, N., Yamamoto, A., Oshitani-Okamoto, S., Ohsumi, Y., & Yoshimori, T. (2004) · Journal of Cell Science · doi:10.1242/jcs.01131 · Cited by 1,394
Self-citationYamamoto, A., Tagawa, Y., Yoshimori, T., Moriyama, Y., Masaki, R., & Tashiro, Y. (1998) · Cell Structure and Function · doi:10.1247/csf.23.33 · Cited by 1,312
Self-citationLysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy
Tanida, I., Minematsu-Ikeguchi, N., Ueno, T., & Kominami, E. (2005) · Autophagy · doi:10.4161/auto.1.2.1697 · Cited by 1,108
Suzuki, K., Kirisako, T., Kamada, Y., Mizushima, N., Noda, T., & Ohsumi, Y. (2001) · The EMBO Journal · doi:10.1093/emboj/20.21.5971 · Cited by 1,060
Self-citationRole of autophagy in temozolomide-induced cytotoxicity for malignant glioma cells
Kanzawa, T., Germano, I. M., Komata, T., Ito, H., Kondo, Y., & Kondo, S. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401359 · Cited by 995
Methods for monitoring autophagy
Mizushima, N. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.02.005 · Cited by 899
Self-citationMethods for Monitoring Autophagy from Yeast to Human
Klionsky, D. J., Cuervo, A. M., & Seglen, P. O. (2007) · Autophagy · doi:10.4161/auto.3678 · Cited by 656
Small molecules enhance autophagy and reduce toxicity in Huntington's disease models
Sarkar, S., Perlstein, E. O., Imarisio, S., Pineau, S., Cordenier, A., Maglathlin, R. L., Webster, J. A., Lewis, T. A., O’Kane, C. J., Schreiber, S. L., et al. (2007) · Nature Chemical Biology · doi:10.1038/nchembio883 · Cited by 604
Kuma, A., Matsui, M., & Mizushima, N. (2007) · Autophagy · doi:10.4161/auto.4012 · Cited by 555
Self-citationCellular autophagy: surrender, avoidance and subversion by microorganisms
Kirkegaard, K., Taylor, M. P., & Jackson, W. T. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro865 · Cited by 444
Induction of Autophagy in Axonal Dystrophy and Degeneration
Wang, Q. J., Ding, Y., Kohtz, S., Mizushima, N., Cristea, I. M., Rout, M. P., Chait, B. T., Zhong, Y., Heintz, N., & Yue, Z. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.2261-06.2006 · Cited by 308
Self-citationIn Vivo and in Vitro Reconstitution of Atg8 Conjugation Essential for Autophagy
Ichimura, Y., Imamura, Y., Emoto, K., Umeda, M., Noda, T., & Ohsumi, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405860200 · Cited by 193
SKD1 AAA ATPase-Dependent Endosomal Transport is Involved in Autolysosome Formation.
Nara, A., Mizushima, N., Yamamoto, A., Kabeya, Y., Ohsumi, Y., & Yoshimori, T. (2002) · Cell Structure and Function · doi:10.1247/csf.27.29 · Cited by 144
Self-citationKuusisto, E., Suuronen, T., & Salminen, A. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4107 · Cited by 131
Nakaso, K., Yoshimoto, Y., Nakano, T., Takeshima, T., Fukuhara, Y., Yasui, K., Araga, S., Yanagawa, T., Ishii, T., & Nakashima, K. (2004) · Brain Research · doi:10.1016/j.brainres.2004.03.029 · Cited by 121
Modifications in P62 occur due to proteasome inhibition in alcoholic liver disease
Bardag-Gorce, F., Francis, T., Nan, L., Li, J., He Lue, Y., French, B. A., & French, S. W. (2005) · Life Sciences · doi:10.1016/j.lfs.2005.04.020 · Cited by 43
Flagged first, then by citations
1 of the 21 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894
“tion independently of traditional autophagy, in a noncanonical autophagic process termed LC3-associated phagocytosis.(1,26,1448) LAP occurs upon engulfment of particles that engage a recep-”
InfluentialSelf-citationMethods in Mammalian Autophagy Research
Mizushima, N., Yoshimori, T., & Levine, B. (2010) · Cell · doi:10.1016/j.cell.2010.01.028 · Cited by 4,497
Self-citationGuidelines for the use and interpretation of assays for monitoring autophagy
Klionsky, D. J., Abdalla, F. C., Abeliovich, H., Abraham, R. T., Acevedo-Arozena, A., Adeli, K., Agholme, L., Agnello, M., Agostinis, P., Aguirre-Ghiso, J. A., et al. (2012) · Autophagy · doi:10.4161/auto.19496 · Cited by 3,996
“In addition to LC3, SQSTM1/p62, or other receptors such as NBR1, can also be used as a protein marker, at least in certain settings.(25,309) The SQSTM1 protein serves as a link between LC3 and ubiquitinated substrates.”
BackgroundMethodInfluentialSelf-citationAutophagy: process and functionPreprint
Mizushima, N. (2007) · Genes & Development · doi:10.1101/gad.1599207 · Cited by 4,104
“One current problem is that this degradation step is rather difficult to measure, although some methods to monitor autophagy flux have been proposed (Tanida et al. 2005; Klionsky et al. 2007; Mizushima and Yoshimori 2007).”
BackgroundSelf-citationAntimicrobial Autophagy: A Conserved Innate Immune Response in Drosophila
Moy, R. H., & Cherry, S. R. (2013) · Journal of Innate Immunity · doi:10.1159/000350326 · Cited by 3,551
Metadata
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › 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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