Cited by 299Metabolism, Diabetes, and CancerAdipose Tissue and MetabolismMuscle Physiology and Disorders

The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.

Activity of LKB1 and AMPK-related kinases in skeletal muscle: effects of contraction, phenformin, and AICAR

Sakamoto, Kei, Göransson, Olga, Hardie, D. Grahame, Alessi, Dario R.·2004·American Journal of Physiology-Endocrinology and Metabolism

DOI 10.1152/ajpendo.00074.2004

Open this paper in CoChat — free account

Abstract

Activation of AMP-activated protein kinase (AMPK) by exercise and metformin is beneficial for the treatment of type 2 diabetes. We recently found that, in cultured cells, the LKB1 tumor suppressor protein kinase activates AMPK in response to the metformin analog phenformin and the AMP mimetic drug 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR). We have also reported that LKB1 activates 11 other AMPK-related kinases. The activity of LKB1 or the AMPK-related kinases has not previously been studied in a tissue with physiological relevance to diabetes. In this study, we have investigated whether contraction, phenformin, and AICAR influence LKB1 and AMPK-related kinase activity in rat skeletal muscle. Contraction in situ, induced via sciatic nerve stimulation, significantly increased AMPKalpha2 activity and phosphorylation in multiple muscle fiber types without affecting LKB1 activity. Treatment of isolated skeletal muscle with phenformin or AICAR stimulated the phosphorylation and activation of AMPKalpha1 and AMPKalpha2 without altering LKB1 activity. Contraction, phenformin, or AICAR did not significantly increase activities or expression of the AMPK-related kinases QSK, QIK, MARK2/3, and MARK4 in skeletal muscle. The results of this study suggest that muscle contraction, phenformin, or AICAR activates AMPK by a mechanism that does not involve direct activation of LKB1. They also suggest that the effects of excercise, phenformin, and AICAR on metabolic processes in muscle may be mediated through activation of AMPK rather than activation of LKB1 or the AMPK-related kinases.

Integrity signals

Registry

Crossref · 10.1152/ajpendo.00074.2004

Cites

32 of 32 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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
The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress
Shaw, R. J., Kosmatka, M., Bardeesy, N., Hurley, R. L., Witters, L. A., DePinho, R. A., & Cantley, L. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308061100 · Cited by 1,797
Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β are upstream kinases in the AMP-activated protein kinase cascade
Hawley, S. A., Boudeau, J., Reid, J. L., Mustard, K. J., Udd, L., Mäkelä, T. P., Alessi, D. R., & Hardie, D. G. (2003) · Journal of Biology · doi:10.1186/1475-4924-2-28 · Cited by 1,694
LKB1 is the upstream kinase in the AMP-activated protein kinase cascade
Woods, A., Johnstone, S. R., Dickerson, K., Leiper, F. C., Fryer, L. G. D., Neumann, D., Schlattner, U., Wallimann, T., Carlson, M., & Carling, D. (2003) · Current Biology · doi:10.1016/j.cub.2003.10.031 · Cited by 1,650
LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR‐1
Lizcano, J. M., Göransson, O., Toth, R., Deak, M., Morrice, N. A., Boudeau, J., Hawley, S. A., Udd, L., Mäkelä, T. P., Hardie, D. G., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600110 · Cited by 1,381
5-Aminoimidazole-4-Carboxamide Ribonucleoside. A Specific Method for Activating AMP-Activated Protein Kinase in Intact Cells?
Corton, J. M., Gillespie, J. G., Hawley, S. A., & Hardie, D. G. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20498.x · Cited by 1,232
The AMP-activated protein kinase cascade – a unifying system for energy control
Carling, D. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.11.005 · Cited by 1,133
The Anti-diabetic Drugs Rosiglitazone and Metformin Stimulate AMP-activated Protein Kinase through Distinct Signaling Pathways
Fryer, L. G. D., Patel, A. P., & Carling, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202489200 · Cited by 1,035
AMP-activated protein kinase, a metabolic master switch: possible roles in Type 2 diabetes
Winder, W. W., & Hardie, D. G. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.277.1.e1 · Cited by 1,000
A Role for AMP-Activated Protein Kinase in Contraction- and Hypoxia-Regulated Glucose Transport in Skeletal Muscle
Mu, J., Brozinick, J. T., Valladares, O., Bucan, M., & Birnbaum, M. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00251-9 · Cited by 924

Show all 32 references

Sorted by citations

AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism
Kahn, B. B., Alquier, T., Carling, D., & Hardie, D. G. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2004.12.003 · Cited by 2,799
AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy
Hardie, D. G. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2249 · Cited by 2,261
AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function
Hardie, D. G. (2011) · Genes & Development · doi:10.1101/gad.17420111 · Cited by 1,638
Exercise, GLUT4, and skeletal muscle glucose uptake
Richter, E. A., & Hargreaves, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00038.2012 · Cited by 1,407
Metformin Inhibits Hepatic Gluconeogenesis in Mice Independently of the LKB1/AMPK Pathway via a Decrease in Hepatic Energy State
Foretz, M., Hébrard, S., Leclerc, J., Zarrinpashneh, E., Soty, M., Mithieux, G., Sakamoto, K., Andreelli, F., & Viollet, B. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40671 · Cited by 1,181
Self-citation
The AMP-activated protein kinase pathway – new players upstream and downstream
Hardie, D. G. (2004) · Journal of Cell Science · doi:10.1242/jcs.01540 · Cited by 1,163
The LKB1 tumor suppressor negatively regulates mTOR signaling
Shaw, R. J., Bardeesy, N. M., Manning, B. D., Lopez, L. V., Kosmatka, M., DePinho, R. A., & Cantley, L. C. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.06.007 · Cited by 1,107
New insights into activation and function of the AMPK
Steinberg, G. R., & Hardie, D. G. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00547-x · Cited by 1,074
The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism
Koo, S., Flechner, L., Qi, L., Zhang, X., Screaton, R. A., Jeffries, S., Hedrick, S. A., Xu, W., Boussouar, F., Brindle, P. K., et al. (2005) · Nature · doi:10.1038/nature03967 · Cited by 1,026
AMPK and SIRT1: a long-standing partnership?
Ruderman, N. B., Julia Xu, X., Nelson, L., Cacicedo, J. M., Saha, A. K., Lan, F., & Ido, Y. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00745.2009 · Cited by 903
AMP-Activated Protein Kinase – Development of the Energy Sensor Concept
Hardie, D. G., Hawley, S. A., & Scott, J. W. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.108944 · Cited by 813
LKB1-Dependent Signaling Pathways
Alessi, D. R., Sakamoto, K., & Bayascas, J. R. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142702 · Cited by 805
Membrane Fatty Acid Transporters as Regulators of Lipid Metabolism: Implications for Metabolic Disease
Glatz, J. F. C., Luiken, J. J. F. P., & Bonen, A. (2010) · Physiological Reviews · doi:10.1152/physrev.00003.2009 · Cited by 776
Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade
Sanders, M. J., Grondin, P., Hegarty, B. D., Snowden, M. A., & Carling, D. (2007) · Biochemical Journal · doi:10.1042/bj20061520 · Cited by 677
AMPK—Sensing Energy while Talking to Other Signaling Pathways
Hardie, D. G. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.09.013 · Cited by 597
Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction
Sakamoto, K., McCarthy, A., Smith, D. P., Green, K. A., Hardie, D. G., Ashworth, A., & Alessi, D. R. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600667 · Cited by 552
AMP Is a True Physiological Regulator of AMP-Activated Protein Kinase by Both Allosteric Activation and Enhancing Net Phosphorylation
Gowans, G. J., Hawley, S. A., Ross, F. A., & Hardie, D. G. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.08.019 · Cited by 531
AMPK: A Key Sensor of Fuel and Energy Status in Skeletal Muscle
Hardie, D. G., & Sakamoto, K. (2006) · Physiology · doi:10.1152/physiol.00044.2005 · Cited by 536
AMPK in skeletal muscle function and metabolism
Kjøbsted, R., Hingst, J. R., Fentz, J., Foretz, M., Sanz, M.-N., Pehmøller, C. K., Shum, M., Marette, A., Mounier, R., Treebak, J. T., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700442r · Cited by 517
AMPK and the biochemistry of exercise: implications for human health and disease
Richter, E. A., & Ruderman, N. B. (2009) · Biochemical Journal · doi:10.1042/bj20082055 · Cited by 481
AMP‐activated protein kinase in the regulation of hepatic energy metabolism: from physiology to therapeutic perspectives
Viollet, B., Guigas, B., Leclerc, J., Hébrard, S., Lantier, L., Mounier, R., Andréelli, F., & Foretz, M. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01970.x · Cited by 498
AMPK: positive and negative regulation, and its role in whole-body energy homeostasis
Hardie, D. G. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.09.004 · Cited by 485
Self-citation
Selective activation of AMPK‐PGC‐1α or PKB‐TSC2‐mTOR signaling can explain specific adaptive responses to endurance or resistance training‐like electrical muscle stimulation
Atherton, P. J., Babraj, J. A., Smith, K., Singh, J., Rennie, M. J., & Wackerhage, H. (2005) · The FASEB Journal · doi:10.1096/fj.04-2179fje · Cited by 475
Mechanism of Action of A-769662, a Valuable Tool for Activation of AMP-activated Protein Kinase
Göransson, O., McBride, A., Hawley, S. A., Ross, F. A., Shpiro, N., Foretz, M., Viollet, B., Hardie, D. G., & Sakamoto, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706536200 · Cited by 452
AMP-activated protein kinase and its downstream transcriptional pathways
Cantó, C., & Auwerx, J. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0454-z · Cited by 421
Tumor necrosis factor α-induced skeletal muscle insulin resistance involves suppression of AMP-kinase signaling
Steinberg, G. R., Michell, B. J., van Denderen, B. J. W., Watt, M. J., Carey, A. L., Fam, B. C., Andrikopoulos, S., Proietto, J., Görgün, C. Z., Carling, D., et al. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.11.005 · Cited by 424
AMP-Activated Protein Kinase as a Drug Target
Hardie, D. G. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105304 · Cited by 411
Important role of the LKB1-AMPK pathway in suppressing tumorigenesis in PTEN-deficient mice
Huang, X., Wullschleger, S., Shpiro, N., McGuire, V. A., Sakamoto, K., Woods, Y. L., Mcburnie, W., Fleming, S., & Alessi, D. R. (2008) · Biochemical Journal · doi:10.1042/bj20080557 · Cited by 396
AMPK alterations in cardiac physiology and pathology: enemy or ally?
Dyck, J. R. B., & Lopaschuk, G. D. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.109389 · Cited by 392
AMPK inhibition in health and disease
Viollet, B., Horman, S., Leclerc, J., Lantier, L., Foretz, M., Billaud, M., Giri, S., & Andreelli, F. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.488215 · Cited by 383
AMP-activated protein kinase: new regulation, new roles?
Carling, D., Thornton, C., Woods, A., & Sanders, M. J. (2012) · Biochemical Journal · doi:10.1042/bj20120546 · Cited by 390
AMP-Activated Protein Kinase: A Target for Drugs both Ancient and Modern
Hardie, D. G., Ross, F. A., & Hawley, S. A. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.08.019 · Cited by 385
A pivotal role for endogenous TGF-β-activated kinase-1 in the LKB1/AMP-activated protein kinase energy-sensor pathway
Xie, M., Zhang, D., Dyck, J. R. B., Li, Y., Zhang, H., Morishima, M., Mann, D. L., Taffet, G. E., Baldini, A., Khoury, D. S., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604708103 · Cited by 358
AMPK integrates nutrient and hormonal signals to regulate food intake and energy balance through effects in the hypothalamus and peripheral tissues
Xue, B., & Kahn, B. B. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.113217 · Cited by 338
Contraction signaling to glucose transport in skeletal muscle
Jessen, N., & Goodyear, L. J. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00175.2005 · Cited by 311
Effect of Acute Exercise on AMPK Signaling in Skeletal Muscle of Subjects with Type 2 Diabetes
Sriwijitkamol, A., Coletta, D. K., Wajcberg, E., Balbontin, G. B., Reyna, S. M., Barrientes, J., Eagan, P. A., Jenkinson, C. P., Cersosimo, E., DeFronzo, R. A., et al. (2007) · Diabetes · doi:10.2337/db06-1119 · Cited by 304
AMP-activated protein kinase: an emerging drug target to regulate imbalances in lipid and carbohydrate metabolism to treat cardio-metabolic diseases
Srivastava, R. A. K., Pinkosky, S. L., Filippov, S. I., Hanselman, J. C., Cramer, C. T., & Newton, R. S. (2012) · Journal of Lipid Research · doi:10.1194/jlr.r025882 · Cited by 308
Exercise-induced histone modifications in human skeletal muscle
McGee, S. L., Fairlie, E., Garnham, A. P., & Hargreaves, M. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.181065 · Cited by 296
Activation and Signaling by the AMP-Activated Protein Kinase in Endothelial Cells
Fisslthaler, B., & Fleming, I. (2009) · Circulation Research · doi:10.1161/circresaha.109.201590 · Cited by 295
Predominant α2/β2/γ3 AMPK activation during exercise in human skeletal muscle
Birk, J. B., & Wojtaszewski, J. F. P. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.120972 · Cited by 293
The regulation of AMP-activated protein kinase by upstream kinases
Carling, D., Sanders, M. J., & Woods, A. (2008) · International Journal of Obesity · doi:10.1038/ijo.2008.124 · Cited by 295
Role of AMP-activated protein kinase in adipose tissue metabolism and inflammation
Bijland, S., Mancini, S. J., & Salt, I. P. (2013) · Clinical Science · doi:10.1042/cs20120536 · Cited by 296
AMPK: Regulating Energy Balance at the Cellular and Whole Body Levels
Hardie, D. G., & Ashford, M. L. J. (2014) · Physiology · doi:10.1152/physiol.00050.2013 · Cited by 280
Phosphorylation of LKB1 at Serine 428 by Protein Kinase C-ζ Is Required for Metformin-Enhanced Activation of the AMP-Activated Protein Kinase in Endothelial Cells
Xie, Z., Dong, Y., Scholz, R., Neumann, D., & Zou, M.-H. (2008) · Circulation · doi:10.1161/circulationaha.107.744490 · Cited by 273
AMP-activated protein kinase: maintaining energy homeostasis at the cellular and whole-body levels
Hardie, D. G. (2014) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071812-161148 · Cited by 281
Role of AMPK in skeletal muscle metabolic regulation and adaptation in relation to exercise
Jørgensen, S. B., Richter, E. A., & Wojtaszewski, J. F. P. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.109942 · Cited by 261
Effect of Maternal Nutrient Restriction in Sheep on the Development of Fetal Skeletal Muscle1
Zhu, M.-J., Ford, S. P., Nathanielsz, P. W., & Du, ‬. (2004) · Biology of Reproduction · doi:10.1095/biolreprod.104.034561 · Cited by 256
New roles for the LKB1→AMPK pathway
Hardie, D. G. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.01.006 · Cited by 256
AMP-activated protein kinase in skeletal muscle: From structure and localization to its role as a master regulator of cellular metabolism
Witczak, C. A., Sharoff, C. G., & Goodyear, L. J. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8244-6 · Cited by 253
Metformin Activates AMP Kinase through Inhibition of AMP Deaminase
Ouyang, J., Parakhia, R. A., & Ochs, R. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.121806 · Cited by 251
The Regulation of Fat Metabolism during Aerobic Exercise
Muscella, A., Stefàno, E., Lunetti, P., Capobianco, L., & Marsigliante, S. (2020) · Biomolecules · doi:10.3390/biom10121699 · Cited by 237
Mechanisms of regulation of SNF1/AMPK/SnRK1 protein kinases
Crozet, P., Margalha, L., Confraria, A., Rodrigues, A., Martinho, C., Adamo, M., Elias, A., & Gonzalez, E. B. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00190 · Cited by 241
AMP‐activated protein kinase: role in metabolism and therapeutic implications
Schimmack, G., DeFronzo, R. A., & Musi, N. (2006) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2005.00561.x · Cited by 231
New strategies in sport nutrition to increase exercise performance
Close, G. L., Hamilton, D. L., Philp, A., Burke, L. M., & Morton, J. P. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.01.016 · Cited by 221
LKB1 and AMPK Family Signaling: The Intimate Link Between Cell Polarity and Energy Metabolism
Jansen, M., ten Klooster, J. P., Offerhaus, G. J. A., & Clevers, H. C. (2009) · Physiological Reviews · doi:10.1152/physrev.00026.2008 · Cited by 233
Deficiency of LKB1 in heart prevents ischemia-mediated activation of AMPKα2 but not AMPKα1
Sakamoto, K., Zarrinpashneh, E., Budas, G. R., Pouleur, A., Dutta, A., Prescott, A. R., Vanoverschelde, J., Ashworth, A., Jovanović, A., Alessi, D. R., et al. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00443.2005 · Cited by 224
Possible CaMKK-dependent regulation of AMPK phosphorylation and glucose uptake at the onset of mild tetanic skeletal muscle contraction
Jensen, T. E., Rose, A. J., Jørgensen, S. B., Brandt, N., Schjerling, P., Wojtaszewski, J. F. P., & Richter, E. A. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00456.2006 · Cited by 216
Role of AMP‐activated protein kinase in the metabolic syndrome and in heart disease
Hardie, D. G. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.11.018 · Cited by 221
Adiponectin Activates AMP-Activated Protein Kinase in Muscle Cells via APPL1/LKB1-Dependent and Phospholipase C/Ca2+/Ca2+/Calmodulin-Dependent Protein Kinase Kinase-Dependent Pathways
Zhou, L., Deepa, S. S., Etzler, J. C., Ryu, J., Mao, X., Fang, Q., Liu, D. D., Torres, J. M., Jia, W., Lechleiter, J. D., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.028357 · Cited by 212
Dual Role of Interleukin-6 in Regulating Insulin Sensitivity in Murine Skeletal Muscle
Nieto-Vazquez, I., Fernández-Veledo, S., de Alvaro, C., & Lorenzo, M. (2008) · Diabetes · doi:10.2337/db07-1062 · Cited by 209
Retracted
Skeletal Muscle-Selective Knockout of LKB1 Increases Insulin Sensitivity, Improves Glucose Homeostasis, and Decreases TRB3
Koh, H.-J., Arnolds, D. E., Fujii, N., Tran, T. T., Rogers, M. J., Jessen, N., Li, Y., Liew, C. W., Ho, R. C., Hirshman, M. F., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00979-06 · Cited by 202
Limitations in anti-obesity drug development: the critical role of hunger-promoting neurons
Dietrich, M. O., & Horváth, T. L. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3739 · Cited by 205
Impaired Activation of AMP-Kinase and Fatty Acid Oxidation by Globular Adiponectin in Cultured Human Skeletal Muscle of Obese Type 2 Diabetics
Chen, M. B., McAinch, A. J., Macaulay, S. L., Castelli, L. A., O’Brien, P. E., Dixon, J. B., Cameron‐Smith, D., Kemp, B. E., & Steinberg, G. R. (2005) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-1980 · Cited by 201
The regulation and function of mammalian AMPK‐related kinases
Bright, N. J., Thornton, C., & Carling, D. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01971.x · Cited by 208
Increase in S6K1 phosphorylation in human skeletal muscle following resistance exercise occurs mainly in type II muscle fibers
Koopman, R., Zorenc, A. H. G., Gransier, R. J. J., Cameron-Smith, D., & van Loon, L. J. C. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00530.2005 · Cited by 196
Phosphorylation and 14‐3‐3 binding of Arabidopsis trehalose‐phosphate synthase 5 in response to 2‐deoxyglucose
Harthill, J. E., Meek, S. E. M., MORRICE, N. A., Peggie, M. W., Borch, J., Wong, B. H. C., & MacKintosh, C. (2006) · The Plant Journal · doi:10.1111/j.1365-313x.2006.02780.x · Cited by 182
AMP-activated protein kinase phosphorylates transcription factors of the CREB family
Thomson, D. M., Herway, S. T., Fillmore, N., Kim, H., Brown, J. D., Barrow, J. R., & Winder, W. W. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00900.2007 · Cited by 187
The orphan nuclear receptor Nur77 regulates LKB1 localization and activates AMPK
Zhan, Y.-Y., Chen, Y., Zhang, Q., Zhuang, J.-J., Tian, M., Chen, H.-Z., Zhang, L.-R., Zhang, H.-K., He, J.-P., Wang, W.-J., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1069 · Cited by 180
Motif affinity and mass spectrometry proteomic approach for the discovery of cellular AMPK targets: Identification of mitochondrial fission factor as a new AMPK substrate
Ducommun, S., Deak, M., Sumpton, D., Ford, R. J., Núñez Galindo, A., Kussmann, M., Viollet, B., Steinberg, G. R., Foretz, M., Dayon, L., et al. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.02.008 · Cited by 167
Self-citation
Regulation of AMP-activated protein kinase by natural and synthetic activators
Hardie, D. G. (2015) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2015.06.002 · Cited by 180
Rosiglitazone suppresses human lung carcinoma cell growth through PPARγ-dependent and PPARγ-independent signal pathways
Han, S., & Roman, J. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0347 · Cited by 170
AMP-Activated Protein Kinase: A Key Stress Signaling Pathway in the Heart
Young, L. H., Li, J., Baron, S. J., & Russell, R. R. (2005) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2005.04.005 · Cited by 165
The LKB1-salt-inducible kinase pathway functions as a key gluconeogenic suppressor in the liver
Patel, K., Foretz, M., Marion, A., Campbell, D. G., Gourlay, R., Boudaba, N., Tournier, E., Titchenell, P. M., Peggie, M. W., Deák, M., et al. (2014) · Nature Communications · doi:10.1038/ncomms5535 · Cited by 171
Molecular Pathways: Is AMPK a Friend or a Foe in Cancer?
Hardie, D. G. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-3300 · Cited by 166
Targeting AMPK: A new therapeutic opportunity in breast cancer
Hadad, S. M., Fleming, S., & Thompson, A. M. (2008) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2008.01.007 · Cited by 158
Tamoxifen-Induced Anorexia Is Associated With Fatty Acid Synthase Inhibition in the Ventromedial Nucleus of the Hypothalamus and Accumulation of Malonyl-CoA
López, M., Lelliott, C. J., Tovar, S. A., Kimber, W. L., Gallego, R., Virtue, S., Blount, M., Vazquez, M. J., Finer, N., Powles, T. J., et al. (2006) · Diabetes · doi:10.2337/db05-1356 · Cited by 151
AMPK: a cellular energy sensor primarily regulated by AMP
Gowans, G. J., & Hardie, D. G. (2014) · Biochemical Society Transactions · doi:10.1042/bst20130244 · Cited by 152
Cannabinoids inhibit energetic metabolism and induce AMPK-dependent autophagy in pancreatic cancer cells
Dando, I., Donadelli, M., Costanzo, C., Dalla Pozza, E., D'Alessandro, A., Zolla, L., & Palmieri, M. (2013) · Cell Death & Disease · doi:10.1038/cddis.2013.151 · Cited by 128
Skeletal muscle and heart LKB1 deficiency causes decreased voluntary running and reduced muscle mitochondrial marker enzyme expression in mice.
Thomson, D. M., Porter, B. B., Tall, J. H., Kim, H.-J., Barrow, J. R., & Winder, W. W. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00366.2006 · Cited by 146
Cellular energy sensing and signaling by AMP-activated protein kinase
Winder, W. W., & Thomson, D. M. (2007) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-007-0008-7 · Cited by 142
Exercise-induced AMPK activity in skeletal muscle: Role in glucose uptake and insulin sensitivity
Friedrichsen, M., Mortensen, B., Pehmøller, C., Birk, J. B., & Wojtaszewski, J. F. P. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.06.013 · Cited by 143
Calmodulin-dependent protein kinase kinase-β activates AMPK without forming a stable complex: synergistic effects of Ca2+ and AMP
Fogarty, S., Hawley, S. A., Green, K. A., Saner, N., Mustard, K. J., & Hardie, D. G. (2009) · Biochemical Journal · doi:10.1042/bj20091372 · Cited by 146
Exploiting the anti-inflammatory effects of AMP-activated protein kinase activation
Salt, I. P., & Palmer, T. M. (2012) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2012.696609 · Cited by 141
Short‐term exercise training in humans reduces AMPK signalling during prolonged exercise independent of muscle glycogen
McConell, G. K., Lee, R. S., Chen, Z., Stepto, N. K., Huynh, N., Stephens, T. J., Canny, B. J., & Kemp, B. E. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.089839 · Cited by 139
AMP-activated protein kinase (AMPK) activating agents cause dephosphorylation of Akt and glycogen synthase kinase-3
King, T. D., Song, L., & Jope, R. S. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.03.005 · Cited by 137
The strange case of AMPK and cancer: Dr Jekyll or Mr Hyde?
Vara‐Ciruelos, D., Russell, F. M., & Hardie, D. G. (2019) · Open Biology · doi:10.1098/rsob.190099 · Cited by 140
Fuel economy in food‐deprived skeletal muscle: signaling pathways and regulatory mechanisms
de Lange, P., Moreno, M., Silvestri, E., Lombardi, A., Goglia, F., & Lanni, A. (2007) · The FASEB Journal · doi:10.1096/fj.07-8527rev · Cited by 137
AMP‐activated protein kinase mediates preconditioning in cardiomyocytes by regulating activity and trafficking of sarcolemmal ATP‐sensitive K+ channels
Sukhodub, A., Jovanović, S., Du, Q., Budas, G. R., Clelland, A. K., Shen, M., Sakamoto, K., Tian, R., & Jovanović, A. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20862 · Cited by 136
Important role for AMPKαl in limiting skeletal muscle cell hypertrophy
Mounier, R., Lantier, L., Leclerc, J., Sotiropoulos, A., Pende, M., Daegelen, D., Sakamoto, K., Foretz, M., & Viollet, B. (2009) · The FASEB Journal · doi:10.1096/fj.08-119057 · Cited by 133
Diminished overload-induced hypertrophy in aged fast-twitch skeletal muscle is associated with AMPK hyperphosphorylation
Thomson, D. M., & Gordon, S. E. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00811.2004 · Cited by 131
Adenosine Monophosphate-Activated Protein Kinase (AMPK) as a New Target for Antidiabetic Drugs: A Review on Metabolic, Pharmacological and Chemical Considerations
Gruzman, A., Babai-Shani, G., & Sasson, S. (2009) · The Review of Diabetic Studies · doi:10.1900/rds.2009.6.13 · Cited by 128
Mechanism of Action of Compound-13: An α1-Selective Small Molecule Activator of AMPK
Hunter, R. W., Foretz, M., Bultot, L., Fullerton, M. D., Deák, M., Ross, F. A., Hawley, S. A., Shpiro, N., Viollet, B., Barron, D., et al. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.05.014 · Cited by 132
AICAR induces phosphorylation of AMPK in an ATM-dependent, LKB1-independent manner
Sun, Y., Connors, K. E., & Yang, D.-Q. (2007) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-007-9575-6 · Cited by 122
Histone modifications and exercise adaptations
McGee, S. L., & Hargreaves, M. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00979.2010 · Cited by 120
14-3-3 cooperates with LKB1 to regulate the activity and localization of QSK and SIK
Al-Hakim, A., Göransson, O., Deák, M., Toth, R. L., Campbell, D. G., MORRICE, N. A., Prescott, A. R., & Alessi, D. R. (2005) · Journal of Cell Science · doi:10.1242/jcs.02670 · Cited by 121
AMP‐ACTIVATED PROTEIN KINASE ACTIVATION AS A STRATEGY FOR PROTECTING VASCULAR ENDOTHELIAL FUNCTION
Zou, M., & Wu, Y. (2007) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2007.04851.x · Cited by 116
Insulin promotes glycogen synthesis in the absence of GSK3 phosphorylation in skeletal muscle
Bouskila, M., Hirshman, M. F., Jensen, J., Goodyear, L. J., & Sakamoto, K. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00481.2007 · Cited by 118
Resveratrol-Induced AMP-Activated Protein Kinase Activation Is Cell-Type Dependent: Lessons from Basic Research for Clinical Application
Lan, F., Weikel, K., Cacicedo, J., & Ido, Y. (2017) · Nutrients · doi:10.3390/nu9070751 · Cited by 112
Ca2+/calmodulin-dependent protein kinase kinase is involved in AMP-activated protein kinase activation by α-lipoic acid in C2C12 myotubes
Shen, Q. W., Zhu, M. J., Tong, J., Ren, J. T., & Du, ‬. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00115.2007 · Cited by 111
Neither LKB1 Nor AMPK Are the Direct Targets of Metformin
Hardie, D. G. (2006) · Gastroenterology · doi:10.1053/j.gastro.2006.07.032 · Cited by 113

Authors: Sakamoto, K., Göransson, O., Hardie, D. G., & Alessi, D. R.
Affiliations: University of Dundee (GB)
ORCID: Sakamoto, Kei
Göransson, Olga
Hardie, D. Grahame
Alessi, Dario R.
Venue: American Journal of Physiology-Endocrinology and Metabolism
Publisher: American Physiological Society
Published: 2004-08
Volume: 287
Issue: 2
Pages: E310-E317
ISSN: 0193-1849 (ISSN-L)
1522-1555
DOI: 10.1152/ajpendo.00074.2004
OpenAlex: W2050427373
Cited by: 299
References: 32
Citations by year: 2025: 6 · 2024: 2 · 2023: 2 · 2022: 6 · 2021: 6 · 2020: 7 · 2019: 7 · 2018: 8 · 2017: 11 · 2016: 13 · 2015: 13 · 2014: 24 · 2013: 14 · 2012: 20
FWCI: 10.06
Type: journal article
Language: en
Open access: closed
Locations: American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (publishedVersion)
Lund University Publications (Lund University) (submittedVersion)
Funders: University of Bristol
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Keywords: LKB1, AMPK, AMPK-related kinases, skeletal muscle, muscle contraction, phenformin, AICAR, AMPKα1, AMPKα2, MARK kinases, physical activity, type 2 diabetes, muscle fiber type, sciatic nerve stimulation
MeSH terms: AMP-Activated Protein Kinase Kinases, Aminoimidazole Carboxamide, Animals, Cells, Cultured, Enzyme Activation, Fibroblasts, HeLa Cells, Humans, Hypoglycemic Agents, Isoenzymes, Male, Multienzyme Complexes, Muscle Contraction, Organ Culture Techniques, Phenformin, Physical Conditioning, Animal, Ribonucleotides, Rats, Wistar, Protein Serine-Threonine Kinases, Mice, Knockout, Muscle, Skeletal, Mice, Rats, AMP-Activated Protein Kinases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Activity of LKB1 and AMPK-related kinases in skeletal muscle: effects of contraction, phenformin, and AICAR

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks