The autophagy initiating kinase ULK1 is regulated via opposing phosphorylation by AMPK and mTOR
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The serine/threonine kinase ULK1 is a mammalian homolog of Atg1, part of the Atg1 kinase complex, which is the most upstream component of the core autophagy machinery conserved from yeast to mammals. In budding yeast, activity of the Atg1 kinase complex is inhibited by TORC1 (target of rapamycin complex 1), but how the counterpart ULK1 complex in mammalian cells is regulated has been unknown. Our laboratories recently discovered that AMPK associates with, and directly phosphorylates, ULK1 on several sites and this modification is required for ULK1 activation after glucose deprivation. In contrast, when nutrients are plentiful, the mTORC1 complex phosphorylates ULK1, preventing its association and activation by AMPK. These studies have revealed a molecular mechanism of ULK1 regulation by nutrient signals via the actions of AMPK and mTORC1.
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AMPK is involved in the suppression of mTOR signaling.
“Endurance training has been shown to inhibit mTOR/p70 S6K signaling and reduce IRS1 serine phosphorylation in rat skeletal muscle [157], and recent studies have demonstrated that AMPK is involved in the suppression of mTOR signaling [39].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [39]
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AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227 · see citing works
Self-citationPhosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy
Egan, D. F., Shackelford, D. B., Mihaylova, M. M., Gelino, S., Kohnz, R. A., Mair, W., Vasquez, D. S., Joshi, A., Gwinn, D. M., Taylor, R., et al. (2011) · Science · doi:10.1126/science.1196371 · Cited by 2,600 · see citing works
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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 · see citing works
Guidelines 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 · see citing works
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · see citing works
Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities
Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.022 · Cited by 1,134 · see citing works
Targeting Autophagy in Cancer: Recent Advances and Future Directions
Amaravadi, R. K., Kimmelman, A. C., & Debnath, J. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-0292 · Cited by 928 · see citing works
AMPK and TOR: The Yin and Yang of Cellular Nutrient Sensing and Growth Control
González, A., Hall, M. N., Lin, S.-C., & Hardie, D. G. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.01.015 · Cited by 797 · see citing works
Autophagy as a promoter of longevity: insights from model organisms
Hansen, M., Rubinsztein, D. C., & Walker, D. W. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0033-y · Cited by 754 · see citing works
Small Molecule Inhibition of the Autophagy Kinase ULK1 and Identification of ULK1 Substrates
Egan, D. F., Chun, M. G. H., Vamos, M., Zou, H., Rong, J., Miller, C. J., Lou, H. J., Raveendra-Panickar, D., Yang, C.-C., Sheffler, D. J., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.05.031 · Cited by 715 · see citing works
Self-citationMammalian Autophagy: How Does It Work?
Bento, C. F., Renna, M., Ghislat, G., Puri, C., Ashkenazi, A., Vicinanza, M., Menzies, F. M., & Rubinsztein, D. C. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014556 · Cited by 692 · see citing works
The role of protein clearance mechanisms in organismal ageing and age-related diseases
Vı́lchez, D., Sáez, I., & Dillin, A. G. (2014) · Nature Communications · doi:10.1038/ncomms6659 · Cited by 684 · see citing works
The Lysosome as a Regulatory Hub
Perera, R. M., & Zoncu, R. (2016) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111315-125125 · Cited by 664 · see citing works
Mechanisms of Autophagy Initiation
Hurley, J. H., & Young, L. N. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044820 · Cited by 655 · see citing works
mTORC1 signaling and the metabolic control of cell growth
Ben‐Sahra, I., & Manning, B. D. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.02.012 · Cited by 641 · see citing works
Interplay between ROS and autophagy in cancer cells, from tumor initiation to cancer therapy
Poillet-Perez, L., Despouy, G., Delage-Mourroux, R., & Boyer-Guittaut, M. (2015) · Redox Biology · doi:10.1016/j.redox.2014.12.003 · Cited by 503 · see citing works
Role of Skeletal Muscle in Insulin Resistance and Glucose Uptake
Merz, K. E., & Thurmond, D. C. (2020) · Comprehensive Physiology · doi:10.1002/cphy.c190029 · Cited by 494 · see citing works
Complex interplay between autophagy and oxidative stress in the development of pulmonary disease
Ornatowski, W., Lü, Q., Yegambaram, M., Flores, A. G., Zemskov, E. A., Maltepe, E., Fineman, J. R., Wang, T., & Black, S. M. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101679 · Cited by 474 · see citing works
TOR Signaling and Nutrient Sensing
Dobrenel, T., Caldana, C., Hanson, J., Robaglia, C., Vincentz, M., Veit, B. E., & Meyer, C. (2016) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-043014-114648 · Cited by 449 · see citing works
Mitochondrial quality control mechanisms as molecular targets in cardiac ageing
Picca, A., Mankowski, R. T., Burman, J. L., Donisi, L., Js, K., Marzetti, E., & Leeuwenburgh, C. (2018) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0059-z · Cited by 392 · see citing works
Autophagy in liver diseases: A review
Qian, H., Chao, X., Williams, J. A. R., Fulte, S., Li, T., Yang, L., & Ding, W. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.100973 · Cited by 377 · see citing works
The Role of Autophagy and Mitophagy in Bone Metabolic Disorders
Wang, S., Deng, Z.-T., Ma, Y.-C., Jin, J., Qi, F., Li, S., Liu, C., Lyu, F.-J., & Zheng, Q. (2020) · International Journal on Biological Sciences · doi:10.7150/ijbs.46627 · Cited by 305 · see citing works
Hexokinase-II Positively Regulates Glucose Starvation-Induced Autophagy through TORC1 Inhibition
Roberts, D. J., Tan‐Sah, V. P., Ding, E., Smith, J. M., & Miyamoto, S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.019 · Cited by 330 · see citing works
Regulation of Liver Metabolism by Autophagy
Madrigal‐Matute, J., & Cuervo, A. M. (2015) · Gastroenterology · doi:10.1053/j.gastro.2015.09.042 · Cited by 312 · see citing works
Molecular logic of mTORC1 signalling as a metabolic rheostat
Valvezan, A. J., & Manning, B. D. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0038-7 · Cited by 295 · see citing works
Growing knowledge of the mTOR signaling network
Huang, K., & Fingar, D. C. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.09.011 · Cited by 301 · see citing works
The role of the autophagy in myocardial ischemia/reperfusion injury
Ma, S., Wang, Y., Chen, Y., & Cao, F. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.05.010 · Cited by 306 · see citing works
Autophagy and mitophagy in the context of doxorubicin-induced cardiotoxicity
Koleini, N., & Kardami, E. (2017) · Oncotarget · doi:10.18632/oncotarget.16944 · Cited by 302 · see citing works
AMPK and Exercise: Glucose Uptake and Insulin Sensitivity
O'Neill, H. M. (2013) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2013.37.1.1 · Cited by 295 · see citing works
Maintenance of metabolic homeostasis by Sestrin2 and Sestrin3
Lee, J. H., Budanov, A. V., Talukdar, S., Park, E. J., Park, H. L., Park, H.-W., Bandyopadhyay, G., Li, N., Aghajan, M., Jang, I., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.08.004 · Cited by 295 · see citing works
Leucine and mTORC1: a complex relationship
Dodd, K. M., & Tee, A. R. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00525.2011 · Cited by 294 · see citing works
Genetic Liver-Specific AMPK Activation Protects against Diet-Induced Obesity and NAFLD
Garcia, D., Hellberg, K., Chaix, A., Wallace, M., Herzig, S., Badur, M. G., Lin, T. C., Shokhirev, M. N., Pinto, A. F. M., Ross, D. S., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2018.12.036 · Cited by 294 · see citing works
Self-citationRole of Skeletal Muscle in Insulin Resistance and Glucose Uptake
Merz, K. E., & Thurmond, D. C. (2020) · Comprehensive physiology · doi:10.1002/j.2040-4603.2020.tb00136.x · Cited by 283 · see citing works
AMPK-dependent phosphorylation of lipid droplet protein PLIN2 triggers its degradation by CMA
Kaushik, S., & Cuervo, A. M. (2016) · Autophagy · doi:10.1080/15548627.2015.1124226 · Cited by 273 · see citing works
Drosophila as a model for ageing
Piper, M. D. W., & Partridge, L. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.09.016 · Cited by 273 · see citing works
LC3-associated phagocytosis at a glance
Heckmann, B. L., & Green, D. R. (2019) · Journal of Cell Science · doi:10.1242/jcs.222984 · Cited by 272 · see citing works
Protein damage, repair and proteolysis
Chondrogianni, N., Petropoulos, I., Grimm, S., Georgila, K., Catalgol, B., Friguet, B., Grune, T., & Gonos, E. S. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.09.001 · Cited by 254 · see citing works
AMPK-dependent phosphorylation is required for transcriptional activation of TFEB and TFE3
Paquette, M., El–Houjeiri, L., Zirden, L. C., Puustinen, P., Blanchette, P., Jeong, H., Dejgaard, K., Siegel, P. M., & Pause, A. (2021) · Autophagy · doi:10.1080/15548627.2021.1898748 · Cited by 260 · see citing works
WIPI proteins: essential PtdIns3 P effectors at the nascent autophagosome
Proikas‐Cezanne, T., Takács, Z., Dönnes, P., & Kohlbacher, O. (2015) · Journal of Cell Science · doi:10.1242/jcs.146258 · Cited by 255 · see citing works
Transcriptional Regulation of Autophagy: Mechanisms and Diseases
Di Malta, C., Cinque, L., & Settembre, C. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00114 · Cited by 255 · see citing works
Lee, D. H., Park, J. S., Lee, Y. S., Han, J., Lee, D., Kwon, S. W., Han, D. H., Lee, Y., & Bae, S. H. (2020) · Autophagy · doi:10.1080/15548627.2020.1712108 · Cited by 249 · see citing works
Autophagy regulation and its role in cancer
Lorin, S., Hamaï, A., Mehrpour, M., & Codogno, P. (2013) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2013.06.007 · Cited by 247 · see citing works
Mehrbod, P., Ande, S. R., Alizadeh, J., Rahimizadeh, S., Shariati, A., Malek, H., Hashemi, M. M., Glover, K. K. M., Sher, A. A., Coombs, K. M., et al. (2019) · Virulence · doi:10.1080/21505594.2019.1605803 · Cited by 240 · see citing works
Metabolic regulation of kisspeptin — the link between energy balance and reproduction
Navarro, V. M. (2020) · Nature Reviews Endocrinology · doi:10.1038/s41574-020-0363-7 · Cited by 240 · see citing works
Exercise Training-Induced Regulation of Mitochondrial Quality
Yan, Z., Lira, V. A., & Greene, N. P. (2012) · Exercise and Sport Sciences Reviews · doi:10.1097/jes.0b013e3182575599 · Cited by 233 · see citing works
Wang, S., Li, H., Yuan, M., Fan, H., & Cai, Z. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.1015500 · Cited by 229 · see citing works
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 211 · see citing works
Self-citationER stress, autophagy, and RNA viruses
Jheng, J.-R., Ho, J., & Horng, J. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00388 · Cited by 210 · see citing works
Autophagy in aging and longevity
Wong, S. Q., Kumar, A. V., Mills, J., & Lapierre, L. R. (2019) · Human Genetics · doi:10.1007/s00439-019-02031-7 · Cited by 204 · see citing works
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 199 · see citing works
Mechanisms and context underlying the role of autophagy in cancer metastasis
Dower, C. M., Wills, C. A., Frisch, S. M., & Wang, H. (2018) · Autophagy · doi:10.1080/15548627.2018.1450020 · Cited by 195 · see citing works
Wei, R., Xiao, Y., Song, Y., Yuan, H., Luo, J. F., & Xu, W. (2019) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-019-1043-0 · Cited by 199 · see citing works
The G Protein-Coupled Taste Receptor T1R1/T1R3 Regulates mTORC1 and Autophagy
Wauson, E., Zaganjor, E., Lee, A.-Y., Guerra, M. L., Ghosh, A. B., Bookout, A. L., Chambers, C. P., Jivan, A., McGlynn, K., Hutchison, M. R., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.001 · Cited by 197 · see citing works
Wang, C., Wang, H., Zhang, D., Luo, W., Liu, R., Xu, D., Diao, L., Liao, L., & Liu, Z. (2018) · Nature Communications · doi:10.1038/s41467-018-05449-1 · Cited by 194 · see citing works
Roles of AMP-activated Protein Kinase in Alzheimer’s Disease
Cai, Z., Yan, L., Li, K., Quazi, S. H., & Zhao, B. (2012) · NeuroMolecular Medicine · doi:10.1007/s12017-012-8173-2 · Cited by 193 · see citing works
Mechanisms of mitochondria and autophagy crosstalk
Rambold, A. S., & Lippincott‐Schwartz, J. (2011) · Cell Cycle · doi:10.4161/cc.10.23.18384 · Cited by 191 · see citing works
Hall, D., Cost, N. G., Hegde, S., Kellner, E., Mikhaylova, O., Stratton, Y., Ehmer, B., Abplanalp, W. A., Pandey, R., Biesiada, J., et al. (2014) · Cancer Cell · doi:10.1016/j.ccell.2014.09.015 · Cited by 187 · see citing works
Eukaryotic elongation factor 2 kinase, an unusual enzyme with multiple roles
Kenney, J. W., Moore, C. E., Xuemin, W., & Proud, C. G. (2014) · Advances in Biological Regulation · doi:10.1016/j.jbior.2014.04.003 · Cited by 182 · see citing works
Lysosome: The metabolic signaling hub
Lamming, D. W., & Bar‐Peled, L. (2018) · Traffic · doi:10.1111/tra.12617 · Cited by 183 · see citing works
Rhee, J. S., Saben, J. L., Mayer, A. L., Schulte, M. B., Shyr, Z. A., Stephens, C., Chi, M. M.-Y., & Moley, K. H. (2016) · Human Reproduction · doi:10.1093/humrep/dew048 · Cited by 182 · see citing works
Zhang, L., Fu, L., Zhang, S., Zhang, J. C., Zhao, Y., Zheng, Y., He, G., Yang, S., Ouyang, L., & Liu, B. (2017) · Chemical Science · doi:10.1039/c6sc05368h · Cited by 179 · see citing works
Myocardial stress and autophagy: mechanisms and potential therapies
Delbridge, L. M. D., Mellor, K. M., TAYLOR, D. J., & Gottlieb, R. A. (2017) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2017.35 · Cited by 176 · see citing works
Untangling Autophagy Measurements
Gottlieb, R. A., Andres, A. M., Sin, J., & TAYLOR, D. J. (2015) · Circulation Research · doi:10.1161/circresaha.116.303787 · Cited by 170 · see citing works
Zhang, X., Wang, Q., Wang, X., Chen, X., Shao, M., Zhang, Q., Guo, D., Yan, W. S., Li, C., Wang, W., et al. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.108599 · Cited by 171 · see citing works
Gallic Acid Regulates Body Weight and Glucose Homeostasis Through AMPK Activation
Doan, K. V., Ko, C. M., Kinyua, A. W., Yang, D. J., Choi, Y., Oh, I. Y., Nguyen, N. M., Ko, A., Choi, J. W., Jeong, Y., et al. (2014) · Endocrinology · doi:10.1210/en.2014-1354 · Cited by 166 · see citing works
The central moTOR of metabolism
Simcox, J., & Lamming, D. W. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.02.024 · Cited by 162 · see citing works
Cell Death in the Developing Brain after Hypoxia-Ischemia
Thornton, C., Leaw, B., Mallard, C. E., Nair, S., Jinnai, M., & Hagberg, H. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00248 · Cited by 163 · see citing works
Role and mechanisms of autophagy in acetaminophen‐induced liver injury
Chao, X., Wang, H., Jaeschke, H., & Ding, W. (2018) · Liver International · doi:10.1111/liv.13866 · Cited by 163 · see citing works
Schmitz, K. J., Ademi, C., Bertram, S., Schmid, K. W., & Baba, H. A. (2016) · World Journal of Surgical Oncology · doi:10.1186/s12957-016-0946-x · Cited by 159 · see citing works
The Life and Death of a Plant Cell
Kabbage, M., Kessens, R., Bartholomay, L. C., & Williams, B. (2017) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-043015-111655 · Cited by 157 · see citing works
The evolution of the TOR pathway and its role in cancer
Beauchamp, E. M., & Platanias, L. C. (2012) · Oncogene · doi:10.1038/onc.2012.567 · Cited by 153 · see citing works
20-hydroxyecdysone upregulatesAtggenes to induce autophagy in the Bombyx fat body
Tian, L., Ma, L., Guo, E., Deng, X., Ma, S., Xia, Q., Cao, Y., & Li, S. (2013) · Autophagy · doi:10.4161/auto.24731 · Cited by 155 · see citing works
mTOR function and therapeutic targeting in breast cancer.
Hare, S. H., & Harvey, A. (2017) · PubMed Central · Cited by 152 · see citing works
Regulation of nutrient-sensitive autophagy by uncoordinated 51-like kinases 1 and 2
McAlpine, F. E., Williamson, L. E., Tooze, S. A., & Chan, E. Y. W. (2013) · Autophagy · doi:10.4161/auto.23066 · Cited by 150 · see citing works
Jamart, C., Naslain, D., Gilson, H., & Francaux, M. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00270.2013 · Cited by 148 · see citing works
Autophagy is essential to support skeletal muscle plasticity in response to endurance exercise
Sanchez, A. M. J., Bernardi, H., Py, G., & Candau, R. B. (2014) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00187.2014 · Cited by 143 · see citing works
Dysfunction of autophagy in high-fat diet-induced non-alcoholic fatty liver disease
Ren, Q., Sun, Q., & Fu, J. (2023) · Autophagy · doi:10.1080/15548627.2023.2254191 · Cited by 147 · see citing works
Aryal, P., Kim, K., Park, P., Ham, S., Cho, J. H., & Song, K. (2014) · FEBS Journal · doi:10.1111/febs.12969 · Cited by 142 · see citing works
AMPK inhibits cardiac hypertrophy by promoting autophagy via mTORC1
Li, Y., Chen, C., Yao, F. J., Su, Q., Liu, D., Xue, R., Dai, G., Fang, R., Zeng, J., Chen, Y., et al. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.06.023 · Cited by 139 · see citing works
AMPK contributes to autophagosome maturation and lysosomal fusion
Jang, M., Park, R., Kim, H.-J., Namkoong, S., Jo, D., Huh, Y. H., Jang, I., Lee, J. I., & Park, J. (2018) · Scientific Reports · doi:10.1038/s41598-018-30977-7 · Cited by 139 · see citing works
The Relationship of Redox With Hallmarks of Cancer: The Importance of Homeostasis and Context
Xing, F., Hu, Q., Qin, Y., Xu, J., Zhang, B., Yu, X., & Wang, W. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.862743 · Cited by 136 · see citing works
Autophagy Dysfunction in Alzheimer’s Disease: Mechanistic Insights and New Therapeutic Opportunities
Di Meco, A., Curtis, M. E., Lauretti, E., & Praticò, D. (2020) · Biological Psychiatry · doi:10.1016/j.biopsych.2019.05.008 · Cited by 133 · see citing works
The AMPK-PPARGC1A pathway is required for antimicrobial host defense through activation of autophagy
Yang, C.-S., Kim, J.-J., Lee, H.-M., Jin, H. S., Lee, S.-H., Park, J.-H., Kim, S. J., Kim, J.-M., Han, Y.-M., Lee, M.-S., et al. (2014) · Autophagy · doi:10.4161/auto.28072 · Cited by 131 · see citing works
Self-citationSurviving change: the metabolic journey of hematopoietic stem cells
Kohli, L., & Passegue, E. A. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.04.001 · Cited by 127 · see citing works
Russo, R., Varano, G. P., Adornetto, A., Nazio, F., Tettamanti, G., Girardello, R., Cianfanelli, V., Cavaliere, F., Morrone, L. A., Corasaniti, M. T., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1044-5 · Cited by 127 · see citing works
Ni, H., Williams, J. A. R., Jaeschke, H., & Ding, W. (2013) · Redox Biology · doi:10.1016/j.redox.2013.08.005 · Cited by 126 · see citing works
Ghislat, G., Patrón, M., Rizzuto, R., & Knecht, E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.365767 · Cited by 126 · see citing works
Kang, L., Xiang, Q., Zhan, S., Song, Y., Wang, K., Zhao, K., Li, S., Shao, Z., Cao, Y., & Zhang, Y. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/7810320 · Cited by 125 · see citing works
Mitochondrial Dysfunction in Lung Pathogenesis
Piantadosi, C. A., & Suliman, H. B. (2016) · Annual Review of Physiology · doi:10.1146/annurev-physiol-022516-034322 · Cited by 122 · see citing works
MiR‐451 is decreased in hypertrophic cardiomyopathy and regulates autophagy by targeting TSC 1
Song, L., Su, M., Wang, S., Zou, Y., Wang, X., Wang, Y., Cui, H., Zhao, P., Hui, R., & Wang, J. (2014) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12380 · Cited by 120 · see citing works
Lysosomes: Signaling Hubs for Metabolic Sensing and Longevity
Savini, M., Zhao, Q., & Wang, M. C. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.08.008 · Cited by 115 · see citing works
Cancer metabolism: New insights into classic characteristics
Kato, Y., Maeda, T., Suzuki, A., & Baba, Y. (2017) · Japanese Dental Science Review · doi:10.1016/j.jdsr.2017.08.003 · Cited by 117 · see citing works
Mitochondrial Ca2+ signals in autophagy
Cárdenas, C., & Foskett, J. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.03.001 · Cited by 114 · see citing works
The Interplay between Ca2+ Signaling Pathways and Neurodegeneration
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Sanchez, A. M. J., Candau, R. B., Csibi, A., Pagano, A. F., Raibon, A., & Bernardi, H. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00125.2012 · Cited by 116 · see citing works
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Xing, Y., Sui, Z., Liu, Y., Wang, M., Wei, X., Lu, Q., Wang, X., Liu, N., Chen, L., Chen, R., et al. (2022) · Basic Research in Cardiology · doi:10.1007/s00395-022-00930-x · Cited by 113 · see citing works
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- Authors
- Egan, D., Kim, J., Shaw, R. J., & Guan, K.-L.
- Affiliations
- Salk Institute for Biological Studies (US)
- University of California San Diego (US)
- Corresponding author
- Shaw, Reuben J.
- Guan, Kun-Liang
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2011-06
- Volume
- 7
- Issue
- 6
- Pages
- 643-644
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- PMC
- PMC3359466
- OpenAlex
- W2070871404
- Cited by
- 627
- References
- 2
- Citations by year
- 2026: 20 · 2025: 28 · 2024: 51 · 2023: 33 · 2022: 53 · 2021: 61 · 2020: 57 · 2019: 54 · 2018: 49 · 2017: 56 · 2016: 41 · 2015: 34 · 2014: 42 · 2013: 19 · 2012: 25
- FWCI
- 21.69
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Autophagy (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (R01CA108941)
- Topics
- Health Sciences › Medicine › Epidemiology › 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 › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- ULK1, autophagy initiation, AMPK, mTORC1, protein phosphorylation, nutrient signaling, glucose deprivation, TOR signaling, kinase regulation
- MeSH terms
- Autophagy-Related Protein-1 Homolog, Mechanistic Target of Rapamycin Complex 1, Adenylate Kinase, Animals, Autophagy, Saccharomycetales, Glucose, Humans, Models, Biological, Phosphorylation, Proteins, Gene Expression Regulation, Fungal, Caenorhabditis elegans, Protein Serine-Threonine Kinases, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, Mice, TOR Serine-Threonine Kinases
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