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Biogenesis and Cargo Selectivity of Autophagosomes
Abstract
Autophagy is a major catabolic pathway in eukaryotes, which is required for the lysosomal/vacuolar degradation of cytoplasmic proteins and organelles. Interest in the autophagy pathway has recently gained momentum largely owing to identification of multiple autophagy-related genes and recognition of its involvement in various physiological conditions. Here we review current knowledge of the molecular mechanisms regulating autophagy in mammals and yeast, specifically the biogenesis of autophagosomes and the selectivity of their cargo recruitment. We discuss the different steps of autophagy, from the signal transduction events that regulate it to the completion of this pathway by fusion with the lysosome/vacuole. We also review research on the origin of the autophagic membrane, the molecular mechanism of autophagosome formation, and the roles of two ubiquitin-like protein families and other structural elements that are essential for this process. Finally, we discuss the various modes of autophagy and highlight their functional relevance for selective degradation of specific cargos.
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“Although autophagic cargo can be trapped passively within the autophagosome in nonselective autophagy, direct substrate recruitment to phagophores in selective autophagy is mediated by a series of receptor proteins (e.g., SQSTM1/p62 [sequestosome 1], NBR1, AMBRA1) that contain both an LC3-interacting region (LIR) and separate motifs for binding polyubiquitinated proteins [41].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [41]
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“Expansion then occurs through maturation of the extending phagophore membrane guided by the ATG12–ATG5-ATG16L1 complex, catalyzing insertion of MAP1LC3/LC3 (microtubule associated protein 1 light chain 3) into the phagophore membrane [40,41].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [41]
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“Before membrane insertion, the unbound and immature LC3 precursor protein (LC3-I) undergoes proteolytic processing by ATG4, and conjugation to phosphatidylethanolamine through ATG7 and ATG3. The resulting mature, lipidated isoform (LC3-II) is incorporated into the phagophore membrane [41].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [41]
Citations
Cites
Pankiv, 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
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
Autophagy regulates lipid metabolism
Singh, R., Kaushik, S., Wang, Y., Xiang, Y., Novak, I., Komatsu, M., Tanaka, K., Cuervo, A. M., & Czaja, M. J. (2009) · Nature · doi:10.1038/nature07976 · Cited by 3,975
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Induction of autophagy and inhibition of tumorigenesis by beclin 1
Liang, X. H., Jackson, S., Seaman, M., Brown, K., Kempkes, B., Hibshoosh, H., & Levine, B. (1999) · Nature · doi:10.1038/45257 · Cited by 3,347
Bjørkøy, 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
de Duve, C., & Wattiaux, R. (1966) · Annual Review of Physiology · doi:10.1146/annurev.ph.28.030166.002251 · Cited by 3,033
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
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835
The Rag GTPases Bind Raptor and Mediate Amino Acid Signaling to mTORC1
Sancak, Y., Peterson, T. R., Shaul, Y. D., Lindquist, R. A., Thoreen, C. C., Bar-Peled, L., & Sabatini, D. M. (2008) · Science · doi:10.1126/science.1157535 · Cited by 2,773
Research works printed but not linked: 2
- Pfeifer U., 1977, Acta Biol. Med. Ger., 36, 1691
- Seglen PO, 1990, Semin. Cell Biol., 1, 441
Cited by
Sorted by citations
Items 201–300 of 466
Puustinen, P., Keldsbo, A., Corcelle-Termeau, E., Ngoei, K., Sønder, S. L., Farkas, T., Kaae Andersen, K., Oakhill, J. S., & Jäättelä, M. (2020) · Autophagy · doi:10.1080/15548627.2019.1710430 · Cited by 57
Autophagy in plant pathogenic fungi
Liu, X., Xu, F., Snyder, J. H., Shi, H., Lu, J., & Lin, F. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.03.022 · Cited by 62
Vacuolin‐1 inhibits autophagy by impairing lysosomal maturation via PIK fyve inhibition
Sano, O., Kazetani, K., Funata, M., Fukuda, Y., Matsui, J., & Iwata, H. (2016) · FEBS Letters · doi:10.1002/1873-3468.12195 · Cited by 63
The lifecycle of skeletal muscle mitochondria in obesity
Pileggi, C. A., Parmar, G., & Harper, M. (2021) · Obesity Reviews · doi:10.1111/obr.13164 · Cited by 61
Huang, Y., Zhen, Y., Chen, Y., Sui, S., & Zhang, L. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115842 · Cited by 59
Liver autophagy: physiology and pathology
Komatsu, M. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs059 · Cited by 61
Liu, Z., Song, Y., Wan, L., Zhang, Y., & Zhou, L.-M. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.02.059 · Cited by 59
Rag GTPase in amino acid signaling
Kim, J., & Kim, E. (2016) · Amino Acids · doi:10.1007/s00726-016-2171-x · Cited by 65
Digesting the genetics of inflammatory bowel disease: Insights from studies of autophagy risk genes
Kabi, A., Nickerson, K. P., Homer, C. R., & McDonald, C. (2011) · Inflammatory Bowel Diseases · doi:10.1002/ibd.21868 · Cited by 57
Mashoof, S., Goodroe, A. E., Du, C., Eubanks, J. O., Jacobs, N., Steiner, J. M., Tizard, I. R., Suchodolski, J. S., & Criscitiello, M. F. (2012) · Mucosal Immunology · doi:10.1038/mi.2012.78 · Cited by 56
The Interplay Between Pattern Recognition Receptors and Autophagy in Inflammation
Zhu, Y., Deng, J. P., Nan, M., Zhang, J., Okekunle, A. P., Li, J., Yu, X., & Wang, P. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-0606-2_6 · Cited by 54
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Yan, Q., Zhang, Y., Wang, Q., & Yuan, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315273 · Cited by 56
Deegan, S., Koryga, I., Glynn, S. A., Gupta, S., Gorman, A. M., & Samali, A. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.11.076 · Cited by 60
Pazhouhi, M., Sariri, R., Rabzia, A., & Khazaei, M. (2016) · PubMed Central · doi:10.22038/ijbms.2016.7472 · Cited by 54
Talabér, G., Miklóssy, G., Oaks, Z., Liu, Y., Tooze, S. A., Chudakov, D. M., Bánki, K., & Perl, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0084392 · Cited by 52
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Kim, J.-E., Ko, A.-R., Hyun, H.-W., Min, S.-J., & Kang, T. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0586-x · Cited by 54
Hosogi, S., Kusuzaki, K., Inui, T., Wang, X., & Marunaka, Y. (2014) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12257 · Cited by 54
Li, L., Chen, X., & Gu, H. (2016) · Oncotarget · doi:10.18632/oncotarget.9330 · Cited by 53
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Wu, X., Won, H., & Rubinsztein, D. C. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130185 · Cited by 49
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Mijaljica, D., Prescott, M., & Devenish, R. J. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13033618 · Cited by 55
Molecular Mechanisms Underlying Heart Failure and Their Therapeutic Potential
Fonseka, O., Gare, S. R., Chen, X., Zhang, J., Alatawi, N. H. O., Ross, C., & Liu, W. (2025) · Cells · doi:10.3390/cells14050324 · Cited by 52
Li, G., Li, C., Xia, M., Ritter, J. K., Gehr, T. W. B., Boini, K. M., & Li, P. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373989 · Cited by 48
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Shpilka, T., Mizushima, N., & Elazar, Z. (2012) · Journal of Cell Science · doi:10.1242/jcs.093757 · Cited by 53
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Sakakibara, K., Eiyama, A., Suzuki, S. W., Sakoh‐Nakatogawa, M., Okumura, N., Tani, M., Hashimoto, A., Nagumo, S., Kondo‐Okamoto, N., Kondo‐Kakuta, C., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201591440 · Cited by 47
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Kim, S., Choi, S., & Kang, D. (2020) · BMB Reports · doi:10.5483/bmbrep.2020.53.5.046 · Cited by 47
Hegde, R. N., Chiki, A., Petricca, L., Martufi, P., Arbez, N., Mouchiroud, L., Auwerx, J. H., Landles, C., Bates, G. P., Singh‐Bains, M. K., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2020104671 · Cited by 50
Döring, T., & Prange, R. (2014) · Cellular Microbiology · doi:10.1111/cmi.12398 · Cited by 47
Sakoh‐Nakatogawa, M., Kirisako, H., Nakatogawa, H., & Ohsumi, Y. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.02.003 · Cited by 44
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Zhang, Z., Xu, X., Ma, J., Wu, J., Wang, Y., Zhou, R., & Han, J. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202628 · Cited by 45
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Gu, H., Shi, X.-X., Liu, C., Wang, C., Sui, N., Zhao, Y., Gong, J., Wang, F., Zhang, H., Li, W., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09430-4 · Cited by 45
Choi, S., & Kim, H. J. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.11.044 · Cited by 44
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Song, Y., Tao, Q., Yu, L., Li, L., Bai, T., Song, X., Hu, H., Li, Y., & Tan, X. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.09.003 · Cited by 42
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Self-citationZientara‐Rytter, K., & Sirko, A. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00013 · Cited by 40
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Kim, N., Choi, S., Yi, N., Lee, T. R., & Lee, A. (2017) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12605 · Cited by 38
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Ha, J., & Kim, J. (2016) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2016.1217996 · Cited by 38
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Xu, C., Chen, X., Sheng, W.-B., & Yang, P. (2019) · Reproductive Toxicology · doi:10.1016/j.reprotox.2019.02.005 · Cited by 37
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Fraiberg, M., Tamim-Yecheskel, B.-C., Kokabi, K., Subic, N., Heimer, G., Eck, F., Nalbach, K., Behrends, C., Ben‐Zeev, B., Shatz, O., et al. (2020) · Autophagy · doi:10.1080/15548627.2020.1852727 · Cited by 36
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Praharaj, P. P., Singh, A., Patra, S., & Bhutia, S. K. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.07.008 · Cited by 34
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Zhou, L., He, X., Gao, B., & Xiong, S. (2015) · Journal of Virology · doi:10.1128/jvi.01028-15 · Cited by 33
Chu, L.-W., Huang, Y.-L., Lee, J.-H., Huang, L.-Y., Chen, W.-J., Lin, Y.-H., Chen, J.-Y., Xiang, R., Lee, C.-K., & Ping, Y.-H. (2013) · Journal of Biomedical Optics · doi:10.1117/1.jbo.19.1.011018 · Cited by 34
Hsueh, Y., Yen, C., Shih, N., Chiang, N., Li, C., & Chen, L. (2012) · Autophagy · doi:10.4161/auto.22802 · Cited by 34
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Chen, Y., He, J., Tian, M., Zhang, S. ‐., Guo, M., Kasimu, R., Wang, J. ‐., & Ouyang, L. (2014) · Cell Proliferation · doi:10.1111/cpr.12145 · Cited by 34
Chen, Z., Liang, H., Yan, X., Liang, Q., Bai, Z., Xie, T., Dai, J., Zhao, X., & Xiao, Y. (2023) · Renal Failure · doi:10.1080/0886022x.2023.2284211 · Cited by 34
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Arnoldi, F., Lorenzo, G. D., Mano, M., Schraner, E. M., Wild, P., Eichwald, C., & Burrone, Ó. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095197 · Cited by 34
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Shimizu, T., Inoue, K.-I., Hachiya, H., Shibuya, N., Aoki, T., & Kubota, K. (2016) · Journal of Hepato-Biliary-Pancreatic Sciences · doi:10.1002/jhbp.364 · Cited by 30
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Wang, K., Chen, B., Yin, T., Zhan, Y., Lü, Y., Zhang, Y., Chen, J., Wu, W., Zhou, S., Mao, W., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20143415 · Cited by 31
Yang, X., Niu, L. N., Pan, Y., Feng, X., Liu, J., Guo, Y., Pan, C., Geng, F., & Tang, X. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.561761 · Cited by 30
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Napoli, M., & Flores, E. R. (2013) · Genes & Development · doi:10.1101/gad.219147.113 · Cited by 34
Loos, B., Klionsky, D. J., du Toit, A., & Hofmeyr, J. S. (2019) · Autophagy · doi:10.1080/15548627.2019.1687211 · Cited by 32
Manfredi, L. H., Paula-Gomes, S., Zanon, N. M., & Kettelhut, Í. D. C. (2017) · Brazilian Journal of Medical and Biological Research · doi:10.1590/1414-431x20176733 · Cited by 30
Ding, H., Caza, M., Dong, Y., Arif, A. A., Horianopoulos, L. C., Hu, G., Johnson, P., & Kronstad, J. W. (2018) · Infection and Immunity · doi:10.1128/iai.00069-18 · Cited by 33
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Poillet-Perez, L., Jacquet, M., Hervouet, É., Gauthier, T., Fraîchard, A., Borg, C., Pallandre, J., Gonzalez, B. J., Ramdani, Y., Boyer‐Guittaut, M., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.19639 · Cited by 32
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Wu, W., Kim, H., Zhang, C., Meng, X.-L., & Wu, Z. (2014) · Medical Oncology · doi:10.1007/s12032-014-0108-3 · Cited by 31
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Wong, M. M.-T., Chan, H.-Y., Aziz, N. A., Ramasamy, T. S., Bong, J. J., Ch’ng, E. S., Armon, S., Peh, S., & Teow, S. (2021) · Molecular Biology Reports · doi:10.1007/s11033-021-06334-9 · Cited by 28
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Winer, H. Y., Fraiberg, M., Abada, A., Dadosh, T., Tamim-Yecheskel, B.-C., & Elazar, Z. (2018) · Nature Communications · doi:10.1038/s41467-018-06275-1 · Cited by 25
Self-citationAberrant Stress Granule Dynamics and Aggrephagy in ALS Pathogenesis
Zhang, Y., Gu, J., & Sun, Q. (2021) · Cells · doi:10.3390/cells10092247 · Cited by 28
Smirnova, J., Fernie, A. R., & Steup, M. (2015) · Springer eBooks · doi:10.1007/978-4-431-55495-0_7 · Cited by 26
Huntingtin facilitates selective autophagy
Gelman, A., Rawet-Slobodkin, M., & Elazar, Z. (2015) · Nature Cell Biology · doi:10.1038/ncb3125 · Cited by 28
Self-citationHuang, J., & Wang, J. (2024) · Molecular Medicine Reports · doi:10.3892/mmr.2024.13378 · Cited by 28
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Metadata
- Authors
- Weidberg, H., Shvets, E., & Elazar, Z.
- Affiliations
- Weizmann Institute of Science (IL)
- Corresponding author
- Weidberg, Hilla
- Shvets, Elena
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2011-07-07
- Volume
- 80
- Issue
- 1
- Pages
- 125-156
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2052470191
- Cited by
- 466
- References
- 227
- Citations by year
- 2026: 4 · 2025: 10 · 2024: 15 · 2023: 14 · 2022: 24 · 2021: 26 · 2020: 21 · 2019: 28 · 2018: 25 · 2017: 31 · 2016: 40 · 2015: 38 · 2014: 46 · 2013: 59 · 2012: 68
- FWCI
- 7.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- 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
- autophagy, autophagosome formation, selective autophagy, autophagosome-lysosome fusion, ubiquitin-like proteins, autophagy-related genes, signal transduction, yeast autophagy, cytoplasmic degradation
- MeSH terms
- Animals, Autophagy, Intracellular Membranes, Phagosomes, Yeasts, Organelles, Signal Transduction, Biomarkers
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