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Nutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy
Open accessAbstract
Autophagy is an intracellular degradation system, by which cytoplasmic contents are degraded in lysosomes. Autophagy is dynamically induced by nutrient depletion to provide necessary amino acids within cells, thus helping them adapt to starvation. Although it has been suggested that mTOR is a major negative regulator of autophagy, how it controls autophagy has not yet been determined. Here, we report a novel mammalian autophagy factor, Atg13, which forms a stable ∼3-MDa protein complex with ULK1 and FIP200. Atg13 localizes on the autophagic isolation membrane and is essential for autophagosome formation. In contrast to yeast counterparts, formation of the ULK1–Atg13–FIP200 complex is not altered by nutrient conditions. Importantly, mTORC1 is incorporated into the ULK1–Atg13–FIP200 complex through ULK1 in a nutrient-dependent manner and mTOR phosphorylates ULK1 and Atg13. ULK1 is dephosphorylated by rapamycin treatment or starvation. These data suggest that mTORC1 suppresses autophagy through direct regulation of the ∼3-MDa ULK1–Atg13–FIP200 complex.
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“The initiation step begins with the dissociation of MTOR (mechanistic target of rapamycin kinase) from the PAS, cued by nutrient starvation or treatment with rapamycin or its various derivatives [36,37].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [37]
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“Under starvation, mTORC1 is suppressed and dissociates from the ULK1–ULK2 complex, allowing ULK1 to be activated by AMPK to induce autophagy”
From Autophagy in kidney homeostasis and disease (2020) · cites this paper as [17]
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Autophagy in the Pathogenesis of Disease
Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069
Autophagy fights disease through cellular self-digestion
Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452
Self-citationTOR signaling in growth and metabolism
Wullschleger, S., Loewith, R., & Hall, M. N. (2006) · Cell · doi:10.1016/j.cell.2006.01.016 · Cited by 5,787
Autophagy: process and functionPreprint
Mizushima, N. (2007) · Genes & Development · doi:10.1101/gad.1599207 · Cited by 4,104
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
Defining the role of mTOR in cancer
Guertin, D. A., & Sabatini, D. M. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.05.008 · Cited by 2,833
Genomic Libraries and a Host Strain Designed for Highly Efficient Two-Hybrid Selection in Yeast
James, P. M., Halladay, J. T., & Craig, E. A. (1996) · Genetics · doi:10.1093/genetics/144.4.1425 · Cited by 2,638
How to Interpret LC3 Immunoblotting
Mizushima, N., & Yoshimori, T. (2007) · Autophagy · doi:10.4161/auto.4600 · Cited by 2,595 · cited 2×
“Because LC3-II inside autophagosomes is degraded in autolysosomes, we could see accumulation of LC3-II more clearly if cells were treated with lysosome protease inhibitors (E64d and pepstatin A; Figure Vol. 20, April 1, 2009 1983 3A, lane 3; Tanida et al., 2005; Mizushima and Yoshimori, 2007).”
BackgroundMethodSelf-citationRavikumar, B., Vacher, C., Berger, Z., Davies, J. E., Luo, S., Oroz, L. G., Scaravilli, F., Easton, D. F., Duden, R., O'Kane, C. J., et al. (2004) · Nature Genetics · doi:10.1038/ng1362 · Cited by 2,347
ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery
Jung, C. H., Jun, C. B., Ro, S.-H., Kim, Y.-M., Otto, N. M., Cao, J., Kundu, M., & Kim, D.-H. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1249 · Cited by 2,025
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Joo, J. H., Dorsey, F. C., Joshi, A., Hennessy-Walters, K. M., Rose, K. L., McCastlain, K., Zhang, J., Iyengar, R., Jung, C. H., Suen, D.-F., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.018 · Cited by 232
Pharmacologic agents targeting autophagy
Vakifahmetoglu-Norberg, H., Xia, H., & Yuan, J. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73937 · Cited by 247
Sheen, J.-H., Zoncu, R., Kim, D., & Sabatini, D. M. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.03.012 · Cited by 250
Research Progress on Mechanism of Podocyte Depletion in Diabetic Nephropathy
Dai, H., Liu, Q., & Liu, B. (2017) · Journal of Diabetes Research · doi:10.1155/2017/2615286 · Cited by 242
Regulation of autophagy by coordinated action of mTORC1 and protein phosphatase 2A
Wong, P.-M., Feng, Y., Wang, J., Shi, R., & Jiang, X. (2015) · Nature Communications · doi:10.1038/ncomms9048 · Cited by 239
A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in autophagy
Yang, M., Liang, C., Swaminathan, K., Herrlinger, S., Lai, F., Shiekhattar, R., & Chen, J.-F. (2016) · Science Advances · doi:10.1126/sciadv.1601167 · Cited by 238
Protein oxidation in aging and the removal of oxidized proteins
Höhn, A., König, J., & Grune, T. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.01.004 · Cited by 253
Tanida, I. (2010) · Microbiology and Immunology · doi:10.1111/j.1348-0421.2010.00271.x · Cited by 253
Autophagy Induction as a Therapeutic Strategy for Neurodegenerative Diseases
Djajadikerta, A., Keshri, S., Tanasa, M. P., Prestil, R., Ryan, L., & Rubinsztein, D. C. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.035 · Cited by 244
When autophagy meets cancer through p62/SQSTM1.
Puissant, A., Fenouille, N., & Auberger, P. (2012) · Europe PMC (PubMed Central) · Cited by 236
Autophagy in tumorigenesis and energy metabolism: friend by day, foe by night
Mathew, R., & White, E. (2011) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2010.12.008 · Cited by 245
Amino Acid Signaling in TOR Activation
Kim, J., & Guan, K. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062209-094414 · Cited by 239
Liang, C.-C., Wang, C., Xu, P., Gan, B., & Guan, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.072389 · Cited by 243
Self-citationEbrahim, N., Ahmed, I. A., Hussien, N. I., Dessouky, A. A., Farid, A., Elshazly, A., Mostafa, O., Gazzar, W. B. E., Sorour, S. M., Seleem, Y., et al. (2018) · Cells · doi:10.3390/cells7120226 · Cited by 236
Regulation of autophagy by phosphatidylinositol 3‐phosphate
Burman, C., & Ktistakis, N. T. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.011 · Cited by 234
Valcourt, J. R., Lemons, J. M. S., Haley, E. M., Kojima, M. L., Demuren, O. O., & Coller, H. A. (2012) · Cell Cycle · doi:10.4161/cc.19879 · Cited by 240
FIP200 is required for the cell-autonomous maintenance of fetal hematopoietic stem cells
Liu, F., Lee, J., Wei, H., Tanabe, O., Engel, J. D., Morrison, S. J., & Guan, J. (2010) · Blood · doi:10.1182/blood-2010-06-288589 · Cited by 240
Self-citationMitochondria in the signaling pathways that control longevity and health span
Akbari, M., Kirkwood, T. B. L., & Bohr, V. A. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100940 · Cited by 234
Autophagy signal transduction by ATG proteins: from hierarchies to networks
Wesselborg, S., & Stork, B. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2034-8 · Cited by 241
Lipids, lysosomes, and autophagy
Jaishy, B. P., & Abel, E. D. (2016) · Journal of Lipid Research · doi:10.1194/jlr.r067520 · Cited by 239
Liu, F., Fang, F., Yuan, H., Yang, D., Chen, Y., Williams, L., Goldstein, S. A., Krebsbach, P. H., & Guan, J. (2013) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.1971 · Cited by 228
Self-citationAbnormal mTOR Activation in Autism
Winden, K. D., Ebrahimi‐Fakhari, D., & Şahin, M. (2018) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-080317-061747 · Cited by 232
Autophagy in aging and neurodegenerative diseases: implications for pathogenesis and therapy
Tan, C., Yu, J., Tan, M., Jiang, T., Zhu, X., & Tan, L. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.11.019 · Cited by 224
Liu, C.-C., Lin, Y.-C., Chen, Y.-H., Chen, C.-M., Pang, L.-Y., Chen, H.-A., Wu, P.-R., Lin, M.-Y., Jiang, S.-T., Tsai, T.-F., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2015.11.001 · Cited by 215
Cancer Cell MetabolismPreprint
Cairns, R. A., Harris, I. S., McCracken, S. A., & Mak, T. W. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.012856 · Cited by 229
AMPK-dependent phosphorylation of ULK1 regulates ATG9 localization
Mack, H. I. D., Zheng, B., Asara, J. M., & Thomas, S. Μ. (2012) · Autophagy · doi:10.4161/auto.20586 · Cited by 227
Yamamoto, H., Fujioka, Y., Suzuki, S. W., Noshiro, D., SUZUKI, H., Kondo‐Kakuta, C., Kimura, Y., Hirano, H., Ando, T., Noda, N. N., et al. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.06.015 · Cited by 230
Autophagy and cancer – issues we need to digest
Liu, E. Y., & Ryan, K. M. (2012) · Journal of Cell Science · doi:10.1242/jcs.093708 · Cited by 225
Vesicular trafficking and autophagosome formation
Longatti, A., & Tooze, S. A. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.39 · Cited by 226
Genome-wide CRISPR screen identifies TMEM41B as a gene required for autophagosome formation
Morita, K., Hama, Y., Izume, T., Tamura, N., Ueno, T., Yamashita, Y., Sakamaki, Y., Mimura, K., Morishita, H., Shihoya, W., et al. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201804132 · Cited by 190
Self-citationDunlop, E. A., Hunt, D. K., Acosta-Jaquez, H. A., Fingar, D. C., & Tee, A. R. (2011) · Autophagy · doi:10.4161/auto.7.7.15491 · Cited by 219
Post-translational modifications of Beclin 1 provide multiple strategies for autophagy regulation
Hill, S. M., Wróbel, L., & Rubinsztein, D. C. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0254-9 · Cited by 226
Puyal, J., Ginet, V., & Clarke, P. G. H. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.03.002 · Cited by 224
Pérez-Pérez, M. E., Florencio, F. J., & Crespo, J. L. (2010) · Plant Physiology · doi:10.1104/pp.109.152520 · Cited by 215
Li, H., Chen, L., Li, J., Zhou, Q., Huang, A., Liu, W., Wang, K., Gao, L., Qi, S., & Lu, Y. (2018) · Journal of Hematology & Oncology · doi:10.1186/s13045-018-0618-0 · Cited by 216
mTORC1 phosphorylates the ULK1-mAtg13-FIP200 autophagy regulatory complex
Chan, E. Y. (2009) · Science Signaling · doi:10.1126/scisignal.284pe51 · Cited by 214
Role of autophagy in histone deacetylase inhibitor-induced apoptotic and nonapoptotic cell death
Gammoh, N., Lam, D., Puente, C., Ganley, I. G., Marks, P. A., & Jiang, X. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204429109 · Cited by 215
Bakula, D., Müller, A. J., Zuleger, T., Takács, Z., Franz‐Wachtel, M., Thost, A.-K., Brigger, D., Tschan, M. P., Frickey, T., Robenek, H., et al. (2017) · Nature Communications · doi:10.1038/ncomms15637 · Cited by 216
Signaling Pathways That Control Muscle Mass
Vainshtein, A., & Sandri, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134759 · Cited by 222
Pungsrinont, T., Kallenbach, J., & Baniahmad, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011088 · Cited by 218
AMPK and autophagy in glucose/glycogen metabolism
Ha, J., Guan, K., & Kim, J. (2015) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2015.08.002 · Cited by 219
Autophagosome formation is initiated at phosphatidylinositol synthase‐enriched ER subdomains
Nishimura, T., Tamura, N., Kono, N., Shimanaka, Y., Arai, H., Yamamoto, H., & Mizushima, N. (2017) · The EMBO Journal · doi:10.15252/embj.201695189 · Cited by 216
Self-citationLi, X., Yang, K., Chen, W., Mai, J., Wu, X.-Q., Sun, T., Wu, R., Jiao, L., Li, D., Ji, J., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1912270 · Cited by 212
Renna, M., Jiménez-Sánchez, M., Sarkar, S., & Rubinsztein, D. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.072181 · Cited by 215
Ma, Y., Su, Q., Yue, C., Zou, H., Zhu, J., Zhao, H., Song, R., & Liu, Z. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113491 · Cited by 214
Roles of mTOR complexes in the kidney: implications for renal disease and transplantation
Fantus, D., Rogers, N. M., Grahammer, F., Huber, T. B., & Thomson, A. W. (2016) · Nature Reviews Nephrology · doi:10.1038/nrneph.2016.108 · Cited by 208
Stressin’ Sestrins take an aging fight
Budanov, A. V., Lee, J. H., & Karin, M. (2010) · EMBO Molecular Medicine · doi:10.1002/emmm.201000097 · Cited by 208
Autophagy in cancer development, immune evasion, and drug resistance
Niu, X., You, Q., Hou, K., Tian, Y., Wei, P., Zhu, Y., Gao, B., Ashrafizadeh, M., Aref, A. R., Kalbasi, A., et al. (2024) · Drug Resistance Updates · doi:10.1016/j.drup.2024.101170 · Cited by 244
Fregno, I., Fasana, E., Bergmann, T. J., Raimondi, A., Loi, M., Soldà, T., Galli, C., D'Antuono, R., Morone, D., Danieli, A., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201899259 · Cited by 207
Autophagy in the physiology and pathology of the central nervous system
Nikoletopoulou, V., Papandreou, M. E., & Tavernarakis, N. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.204 · Cited by 206
Research progress of mTOR inhibitors
Chen, Y., & Zhou, X. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112820 · Cited by 219
New Autophagy Reporter Mice Reveal Dynamics of Proximal Tubular Autophagy
Li, L., Wang, Z. V., Hill, J. A., & Lin, F. (2014) · Journal of the American Society of Nephrology · doi:10.1681/asn.2013040374 · Cited by 206
Organelle-Specific Initiation of Autophagy
Sica, V., Galluzzi, L., Bravo-San Pedro, J. M., Izzo, V., Maiuri, M. C., & Kroemer, G. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.021 · Cited by 205
Budanov, A. V. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3530 · Cited by 208
mTOR-Dependent Cell Survival MechanismsPreprint
Hung, C., García-Haro, L., Sparks, C. A., & Guertin, D. A. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008771 · Cited by 215
Autophagy in Alzheimer’s disease
Zare-shahabadi, A., Masliah, E., Johnson, G. V. W., & Rezaei, N. (2015) · Reviews in the Neurosciences · doi:10.1515/revneuro-2014-0076 · Cited by 204
Therapeutic targeting of autophagy in neurodegenerative and infectious diseases
Rubinsztein, D. C., Bento, C. F., & Deretic, V. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20150956 · Cited by 202
Targeting molecules to medicine with mTOR, autophagy and neurodegenerative disorders
Maiese, K. (2015) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.12804 · Cited by 202
Autophagy: Regulation and role in disease
Meijer, A. J., & Codogno, P. (2009) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360903044068 · Cited by 215
Phosphorylation of ULK1 by AMPK regulates translocation of ULK1 to mitochondria and mitophagy
Tian, W., Li, W., Chen, Y., Yan, Z., Huang, X., Zhuang, H., Zhong, W., Chen, Y., Wu, W., Lin, C., et al. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.05.020 · Cited by 210
Mutant HTT (huntingtin) impairs mitophagy in a cellular model of Huntington disease
Franco-Iborra, S., Plaza‐Zabala, A., Montpeyó, M., Sebastián, D., Vila, M., & Martínez‐Vicente, M. (2020) · Autophagy · doi:10.1080/15548627.2020.1728096 · Cited by 205
Autophagy in health and disease. 1. Regulation and significance of autophagy: an overview
Mehrpour, M., Esclatine, A., Beau, I., & Codogno, P. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00507.2009 · Cited by 211
Rodríguez‐Rocha, H., García‐García, A., Panayiotidis, M. I., & Franco, R. (2011) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2011.03.007 · Cited by 205
The ubiquitin-proteasome system and autophagy: Coordinated and independent activities
Cohen‐Kaplan, V., Livneh, I., Avni, N., Cohen-Rosenzweig, C., & Ciechanover, A. J. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.019 · Cited by 205
Histone deacetylase inhibitors induce autophagy through FOXO1-dependent pathways
Zhang, J., Ng, S., Wang, J., Zhou, J., Tan, S.-H., Yang, N., Lin, Q., Xia, D., & Shen, H. (2015) · Autophagy · doi:10.1080/15548627.2015.1023981 · Cited by 199
Tumor Suppression and Promotion by Autophagy
Ávalos, Y., Canales, J., Bravo, R., Criollo, A., Lavandero, S., & Quest, A. F. G. (2014) · BioMed Research International · doi:10.1155/2014/603980 · Cited by 203
Jia, J., Bissa, B., Brecht, L., Allers, L., Choi, S. W., Gu, Y., Zbinden, M., Burge, M. R., Timmins, G. S., Hallows, K. R., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2019.12.028 · Cited by 198
Glynn, E. L., Fry, C. S., Drummond, M. J., Timmerman, K. L., Dhanani, S., Volpi, E., & Rasmussen, B. B. (2010) · The Journal of Nutrition · doi:10.3945/jn.110.127647 · Cited by 194
Role and regulation of autophagy in cancer
Rakesh, R., Dharshini, L. C. P., Sakthivel, K. M., & Rasmi, R. R. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166400 · Cited by 198
Atomistic Autophagy: The Structures of Cellular Self-Digestion
Hurley, J. H., & Schulman, B. A. (2014) · Cell · doi:10.1016/j.cell.2014.01.070 · Cited by 197
Martin, K. R., Celano, S. L., Solitro, A. R., Günaydin, H., Scott, M., O’Hagan, R. C., Shumway, S. D., Fuller, P. H., & MacKeigan, J. P. (2018) · iScience · doi:10.1016/j.isci.2018.09.012 · Cited by 196
Autophagy and ALS: mechanistic insights and therapeutic implications
Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189
Showkat, M., Beigh, M. A., & Andrabi, K. I. (2014) · Molecular Biology International · doi:10.1155/2014/686984 · Cited by 196
Tumorigenesis in tuberous sclerosis complex is autophagy and p62/sequestosome 1 (SQSTM1)-dependent
Parkhitko, A. A., Myachina, F., Morrison, T. A., Hindi, K. M., Auricchio, N., Karbowniczek, M., Wu, J. J., Finkel, T., Kwiatkowski, D. J., Yu, J. J., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1104361108 · Cited by 193
Autophagy in tumour suppression and promotion
Brech, A., Ahlquist, T. C., Lothe, R. A., & Stenmark, H. (2009) · Molecular Oncology · doi:10.1016/j.molonc.2009.05.007 · Cited by 194
The requirement of uncoordinated 51-like kinase 1 (ULK1) and ULK2 in the regulation of autophagy
Lee, E.-J., & Tournier, C. (2011) · Autophagy · doi:10.4161/auto.7.7.15450 · Cited by 186
Autophagic and endo-lysosomal dysfunction in neurodegenerative disease
Malik, B. R., Maddison, D. C., Smith, G. A., & Peters, O. M. (2019) · Molecular Brain · doi:10.1186/s13041-019-0504-x · Cited by 187
FIP200 regulates targeting of Atg16L1 to the isolation membrane
Nishimura, T., Kaizuka, T., Cadwell, K., Sahani, M. H., Saitoh, T., Akira, S., Virgin, H. W., & Mizushima, N. (2013) · EMBO Reports · doi:10.1038/embor.2013.6 · Cited by 189
Self-citationThe Noncanonical Role of ULK/ATG1 in ER-to-Golgi Trafficking Is Essential for Cellular Homeostasis
Joo, J. H., Wang, B., Frankel, E., Ge, L., Xu, L., Iyengar, R., Li-Harms, X., Wright, C., Shaw, T. I., Lindsten, T., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.04.020 · Cited by 158
The interplay between autophagy and ROS in tumorigenesis
Kongara, S., & Karantza, V. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00171 · Cited by 186
How do ESCRT proteins control autophagy?
Rusten, T. E., & Stenmark, H. (2009) · Journal of Cell Science · doi:10.1242/jcs.050021 · Cited by 209
Mammalian macroautophagy at a glance
Ravikumar, B., Futter, M., Jahreiss, L., Korolchuk, V. I., Lichtenberg, M., Luo, S., Massey, D. C. O., Menzies, F. M., Narayanan, U., Renna, M., et al. (2009) · Journal of Cell Science · doi:10.1242/jcs.031773 · Cited by 196
Aurora kinase A inhibition-induced autophagy triggers drug resistance in breast cancer cells
Zou, Z., Yuan, Z., Zhang, Q., Long, Z., Chen, J., Tang, Z., Zhu, Y., Chen, S., Xu, J., Yan, M., et al. (2012) · Autophagy · doi:10.4161/auto.22110 · Cited by 184
Wang, Q., Liang, B., Shirwany, N. A., & Zou, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017234 · Cited by 187
Current knowledge of the pre‐autophagosomal structure (PAS)
Suzuki, K., & Ohsumi, Y. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.001 · Cited by 184
Regulation of Autophagy by Kinases
Sridharan, S., Jain, K., & Basu, A. (2011) · Cancers · doi:10.3390/cancers3022630 · Cited by 189
Age-related macular degeneration: A two-level model hypothesis
Rozing, M. P., Durhuus, J. A., Nielsen, M. K., Subhi, Y., Kirkwood, T. B. L., Westendorp, R. G., & Sørensen, T. L. (2019) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2019.100825 · Cited by 188
Regulation of Autophagy By Signaling Through the Atg1/ULK1 Complex
Papinski, D., & Kraft, C. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.03.030 · Cited by 186
Accumulation of autophagosomes confers cytotoxicity
Button, R. W., Roberts, S. L., Willis, T. L., Hanemann, C. O., & Luo, S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.782276 · Cited by 186
Gao, W., Shen, Z., Shang, L., & Wang, X. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.33 · Cited by 178
DAP1, a Novel Substrate of mTOR, Negatively Regulates Autophagy
Koren, I., Reem, E., & Kimchi, A. (2010) · Current Biology · doi:10.1016/j.cub.2010.04.041 · Cited by 188
Autophagy as a therapeutic target in cardiovascular disease
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Regulation of Body Size and Growth Control
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Metadata
- Authors
- Hosokawa, N., Hara, T., Kaizuka, T., Kishi, C., Takamura, A., Miura, Y., Iemura, S.-I., Natsume, T., Takehana, K., Yamada, N., Guan, J.-L., Oshiro, N., & Mizushima, N.
- Affiliations
- Tokyo Medical and Dental University (JP)
- National Institute of Advanced Industrial Science and Technology (JP)
- Exploratory Research, Pharmaceutical Research Laboratory, and
- Ajinomoto (Japan) (JP)
- University of Michigan (US)
- Biosignal Research Center, Kobe University (JP)
- Venue
- Molecular Biology of the Cell
- Published
- 2009-04
- Volume
- 20
- Issue
- 7
- Pages
- 1981-1991
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC2663915
- OpenAlex
- W2156144699
- Cited by
- 2,076
- References
- 54
- Citations by year
- 2026: 68 · 2025: 81 · 2024: 133 · 2023: 128 · 2022: 139 · 2021: 171 · 2020: 154 · 2019: 132 · 2018: 114 · 2017: 128 · 2016: 132 · 2015: 142 · 2014: 115 · 2013: 112 · 2012: 110
- FWCI
- 73.07
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular Biology of the Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of Tokyo
- Tokyo Medical and Dental University
- 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 › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- autophagy, mTORC1, ULK1, ATG13, FIP200, autophagosome formation, nutrient signaling, mTOR phosphorylation, rapamycin, starvation, lysosomal degradation
- MeSH terms
- Autophagy-Related Proteins, Autophagy-Related Protein-1 Homolog, Mechanistic Target of Rapamycin Complex 1, Amino Acids, Animals, Autophagy, Cell Line, Cell Membrane, Humans, Molecular Weight, Phosphorylation, Protein Binding, Protein Kinases, Proteins, Transcription Factors, Protein Serine-Threonine Kinases, Protein Transport, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Mice, TOR Serine-Threonine Kinases
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