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AMP-activated protein kinase and its downstream transcriptional pathways
Open accessAbstract
The AMP-activated protein kinase (AMPK) is a key regulator of catabolic versus anabolic processes. Its properties as an energy sensor allow it to couple the energy status of the cell to the metabolic environment. These adaptations not only take place through the acute modulation of key metabolic enzymes via direct phosphorylation, but also through a slower transcriptional adaptative response. The question of how AMPK regulates the expression of a number of gene sets, such as those related to mitochondrial biogenesis, energy production and oxidative protection, is only beginning to be elucidated, and still many questions remain to be answered. In this review we will try to integrate our current knowledge on how AMPK regulates transcription in muscle and liver, which will serve as examples to illustrate the major advances in the field and the key challenges ahead.
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“Activation of AMPK increases mitochondrial chemical energy generation by increasing the AMP to ATP ratio236.”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [236]
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“This two-step activation of PGC-1α might be a conserved mechanism for AMPK to confer specificity among the various targets of SIRT1 (Canto & Auwerx, 2010).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Canto & Auwerx, 2010
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International Union of Pharmacology: Approaches to the Nomenclature of Voltage-Gated Ion Channels
Catterall, W. A., Chandy, K. G., Clapham, D. E., Gutman, G. A., Hofmann, F., Harmar, A. J., Abernethy, D. R., & Spedding, M. (2003) · Pharmacological Reviews · doi:10.1124/pr.55.4.5 · Cited by 7,126
Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action
Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652
Resveratrol improves health and survival of mice on a high-calorie diet
Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290
Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139
Lagouge, M., Argmann, C., Gerhart-Hines, Z., Meziane, H., Lerin, C., Daussin, F., Messadeq, N., Milne, J., Lambert, P., Elliott, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.11.013 · Cited by 4,057
Self-citationTSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914
A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis
Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864
AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849
Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510
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Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008
Self-citationHe, J., Zhang, P., Shen, L., Niu, L., Tan, Y., Chen, L., Zhao, Y., Bai, L., Hao, X., Li, X., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176356 · Cited by 1,135
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Amorim, J. A., Coppotelli, G., Rolo, A. P., Palmeira, C. M., Ross, J. M., & Sinclair, D. A. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-021-00626-7 · Cited by 990
Salminen, A., Hyttinen, J. M. T., & Kaarniranta, K. (2011) · Journal of Molecular Medicine · doi:10.1007/s00109-011-0748-0 · Cited by 866
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Salminen, A., & Kaarniranta, K. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2011.12.005 · Cited by 860
Mihaylova, M. M., Vasquez, D. S., Ravnskjaer, K., Denechaud, P.-D., Yu, R. T., Alvarez, J. G., Downes, M., Evans, R. M., Montminy, M., & Shaw, R. J. (2011) · Cell · doi:10.1016/j.cell.2011.03.043 · Cited by 533
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Kulik, A., Wawer, I., Krzywińska, E., Bucholc, M., & Dobrowolska, G. (2011) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2011.0091 · Cited by 509
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“For example, PGC-1α is one well-established target of SIRT1 that acts as a master orchestrator of mitochondrial biogenesis [47].”
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Arciuch, V. G. A., Elguero, M. E., Poderoso, J. J., & Carreras, M. C. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4085 · Cited by 449
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Cantó, C., & Auwerx, J. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.003905 · Cited by 433
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Carling, D., Mayer, F. V., Sanders, M. J., & Gamblin, S. J. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.610 · Cited by 387
Yang, X., Xu, S., Qian, Y., & Xiao, Q. (2017) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2017.03.003 · Cited by 421
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Dönmez, G., & Outeiro, T. F. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201302451 · Cited by 419
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Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383
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Yang, W., Tao, Y., Wu, Y., Zhao, X., Ye, W., Zhao, D., Fu, L., Tian, C., Yang, J., He, F., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09046-8 · Cited by 367
Ramchandani, D., Berisa, M., Tavarez, D. A., Li, Z., Miele, M. M., Bai, Y., Lee, S. B., Ban, Y., Dephoure, N., Hendrickson, R. C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27559-z · Cited by 317
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Viscomi, C. F., Bottani, E., Civiletto, G., Cerutti, R., Moggio, M. G., Fagiolari, G., Schon, E. A., Lamperti, C., & Zeviani, M. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.04.011 · Cited by 302
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Cantó, C., & Auwerx, J. (2011) · Physiology · doi:10.1152/physiol.00010.2011 · Cited by 282
Self-citationFree radical biology for medicine: learning from nonalcoholic fatty liver disease
Serviddio, G., Bellanti, F., & Vendemiale, G. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.174 · Cited by 272
Cokorinos, E., Delmore, J. E., Reyes, A. R., Albuquerque, B., Kjøbsted, R., Eskesen, N. O., Tran, J.-L., Jatkar, A., Cialdea, K., Esquejo, R. M., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.04.010 · Cited by 272
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Cantó, C., Sauve, A. A., & Bai, P. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.004 · Cited by 246
Self-citationFerretta, A., Gaballo, A., Tanzarella, P., Piccoli, C., Capitanio, N., Nico, B., Annese, T., Paola, M. D., Dell’Aquila, C., Mari, M. D., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.02.010 · Cited by 243
Uittenbogaard, M. N., & Chiaramello, A. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140305224906 · Cited by 246
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Wang, X. X., Wang, D., Luo, Y., Myakala, K., Dobrinskikh, E., Rosenberg, A. Z., Levi, J., Kopp, J. B., Field, A. P., Hill, A., et al. (2017) · Journal of the American Society of Nephrology · doi:10.1681/asn.2017020222 · Cited by 232
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Gao, C., Wang, Y., Broaddus, R. R., Sun, L., Xue, F., & Zhang, W. (2017) · Oncotarget · doi:10.18632/oncotarget.23695 · Cited by 227
AMP‐activated protein kinase: a potential player in Alzheimer’s disease
Salminen, A., Kaarniranta, K., Haapasalo, A., Soininen, H. S., & Hiltunen, M. O. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07331.x · Cited by 224
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Bonet, M. L., Ribot, J., & Palou, A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.06.001 · Cited by 218
Nesti, L., & Natali, A. (2017) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2017.04.009 · Cited by 211
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Ghillebert, R., Swinnen, E., Wen, J., Vandesteene, L., Ramon, M., Norga, K., Rolland, F., & Winderickx, J. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08315.x · Cited by 205
Bartlett, J. D., Joo, C.-H., Jeong, T.-S., Louhelainen, J., Cochran, A. J. R., Gibala, M. J., Gregson, W. A., Close, G. L., Drust, B., & Morton, J. P. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01040.2011 · Cited by 210
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Altman, B. J., & Rathmell, J. C. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008763 · Cited by 204
Xie, W., Gu, D., Li, J., Cui, K., & Zhang, Y. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024520 · Cited by 183
Wu, S., & Wei, Y. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.09.014 · Cited by 182
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Gusdon, A. M., Song, K., & Qu, S. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/637027 · Cited by 172
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Curry, D. W., Stutz, B., Andrews, Z. B., & Elsworth, J. D. (2018) · Journal of Parkinson s Disease · doi:10.3233/jpd-171296 · Cited by 160
Wu, S., Wu, Y., Wu, T.-P., & Wei, Y. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.034 · Cited by 164
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Tong, W., Wang, Q., Sun, D., & Suo, J. (2016) · Oncology Letters · doi:10.3892/ol.2016.5148 · Cited by 131
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Foretz, M., & Viollet, B. (2010) · Journal of Hepatology · doi:10.1016/j.jhep.2010.09.014 · Cited by 123
Lu, J., Shi, J., Li, M., Gui, B., Fu, R., Yao, G., Duan, Z., Lv, Z., Yang, Y., Chen, Z., et al. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.01.042 · Cited by 119
Wilkins, H., Harris, J. L., Carl, S. M., Lezi, E., Lu, J., Selfridge, J. E., Roy, N., Hutfles, L. J., Koppel, S. J., Morris, J. K., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu371 · Cited by 119
AMP-activated protein kinase pathway and bone metabolism
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Tartarin, P., Guibert, E., Touré, A., Ouiste, C., Leclerc, J., Sanz, N., Brière, S., Dacheux, J., Delaleu, B., McNEILLY, J. R., et al. (2012) · Endocrinology · doi:10.1210/en.2011-1911 · Cited by 111
Li, J., Yu, S., Jia, Y., Shi, T., & Wang, P. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/7584691 · Cited by 101
Ma, R., Yi, B., Riker, A. I., & Xi, Y. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-00508-0 · Cited by 104
Blättler, S. M., Verdeguer, F., Liesa, M., Cunningham, J. T., Vogel, R. O., Chim, H., Liu, H., Romanino, K., Shirihai, O. S., Vazquez, F., et al. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00337-12 · Cited by 100
Salminen, A., Kauppinen, A., & Kaarniranta, K. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.03.009 · Cited by 100
Chen, R. R., Yung, M. M. H., Yang, X., Zhan, S., Leung, L. L., Liang, R. R., Leung, T. H. Y., Yang, H., Xu, D., Sharma, R., et al. (2019) · Communications Biology · doi:10.1038/s42003-019-0508-1 · Cited by 97
Pasinetti, G. M., Wang, J., Marambaud, P., Ferruzzi, M. G., Gregor, P., Knable, L. A., & Ho, L. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.08.014 · Cited by 99
Jadiya, P., Garbincius, J. F., & Elrod, J. W. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01224-4 · Cited by 94
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Salvatore, T., Galiero, R., Caturano, A., Vetrano, E., Rinaldi, L., Coviello, F., Martino, A. D., Albanese, G., Marfella, R., Sardu, C., et al. (2021) · Biomolecules · doi:10.3390/biom11121834 · Cited by 99
de Kreutzenberg, S. V., Ceolotto, G., Cattelan, A. M., Pagnin, E., Mazzucato, M., Garagnani, P., Borelli, V., Bacalini, M. G., Franceschi, C., Fadini, G. P., et al. (2015) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2015.03.007 · Cited by 94
Barcena, M. L., Pozdniakova, S., Kühl, A. A., Baczkó, I., Ladilov, Y. V., & Regitz‐Zagrosek, V. (2019) · Aging · doi:10.18632/aging.101881 · Cited by 96
The role of hydrogen sulfide in aging and age-related pathologies
Perridon, B. W., Leuvenink, H. G. D., Hillebrands, J., van Goor, H., & Bos, E. M. (2016) · Aging · doi:10.18632/aging.101026 · Cited by 90
LKB1 deficiency-induced metabolic reprogramming in tumorigenesis and non-neoplastic diseases
Zhang, Y., Meng, Q., Sun, Q., Xu, Z., Zhou, H., & Wang, Y. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101131 · Cited by 91
MicroRNA Modulation of Cholesterol Homeostasis
Fernández-Hernando, C., & Moore, K. J. (2011) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.111.226688 · Cited by 89
Resveratrol’s Anti-Cancer Effects through the Modulation of Tumor Glucose Metabolism
Brockmueller, A., Sameri, S., Líšková, A., Zhai, K., Varghese, E., Samuel, S. M., Büsselberg, D., Kubatka, P., & Shakibaei, M. (2021) · Cancers · doi:10.3390/cancers13020188 · Cited by 89
Nepal, S., & Park, P. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.05.013 · Cited by 84
Chowdhury, S. K. R., Dobrowsky, R. T., & Fernyhough, P. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.06.007 · Cited by 82
Ma, J., Wang, Z., Zhao, J., Miao, W., Ye, T., & Chen, A. (2018) · Medical Science Monitor · doi:10.12659/msm.905703 · Cited by 84
Xiao, S., Jiang, S., Qian, D., & Duan, J. (2019) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-019-10312-4 · Cited by 89
Terry, L. J., Vastag, L., Rabinowitz, J. D., & Shenk, T. (2012) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1200494109 · Cited by 87
Wan, J., Zhang, Y., Yang, D., Liang, Y., Yang, L., Hu, S., Liu, Z., Fang, Q., Tian, S., & Ding, Y. (2021) · Hepatology · doi:10.1002/hep.32068 · Cited by 85
Li, H., Liang, J., Han, M., & Gao, Z. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.03.004 · Cited by 85
Ljubicic, V., Burt, M., & Jasmin, B. J. (2013) · The FASEB Journal · doi:10.1096/fj.13-238071 · Cited by 82
Chen, J., Zhu, Y., Zhang, W., Peng, X., Zhou, J., Li, F., Han, B., Liu, X., Ou, Y., & Yu, X. (2018) · BMC Cancer · doi:10.1186/s12885-018-4231-y · Cited by 78
Yu, X., & Li, G. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.08.009 · Cited by 78
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Metadata
- Authors
- Cantó, C., & Auwerx, J.
- Affiliations
- École Polytechnique Fédérale de Lausanne (CH)
- Corresponding author
- Auwerx, Johan
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2010-07-17
- Volume
- 67
- Issue
- 20
- Pages
- 3407-3423
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC3622821
- OpenAlex
- W2067872036
- Cited by
- 421
- References
- 183
- Citations by year
- 2026: 17 · 2025: 28 · 2024: 19 · 2023: 23 · 2022: 20 · 2021: 24 · 2020: 25 · 2019: 23 · 2018: 28 · 2017: 32 · 2016: 20 · 2015: 27 · 2014: 25 · 2013: 30 · 2012: 33
- FWCI
- 3.08
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- reroDoc Digital Library (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-59820, P01DK059820)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- AMPK, transcriptional regulation, energy sensing, mitochondrial biogenesis, muscle, liver, metabolic adaptation, gene expression regulation
- MeSH terms
- Animals, Humans, Models, Biological, Transcription, Genetic, Signal Transduction, AMP-Activated Protein Kinases
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