Cited by 1,589Metabolism, Diabetes, and CancerProtein Kinase Regulation and GTPase SignalingPI3K/AKT/mTOR signaling in cancer

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Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase

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Hawley, Simon A., Pan, David A., Mustard, Kirsty J., Ross, Louise, Bain, Jenny, Edelman, Arthur M., Frenguelli, Bruno G., Hardie, D. Grahame·2005·Cell Metabolism

DOI 10.1016/j.cmet.2005.05.009

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Abstract

The AMP-activated protein kinase (AMPK) is a critical regulator of energy balance at both the cellular and whole-body levels. Two upstream kinases have been reported to activate AMPK in cell-free assays, i.e., the tumor suppressor LKB1 and calmodulin-dependent protein kinase kinase. However, evidence that this is physiologically relevant currently only exists for LKB1. We now report that there is a significant basal activity and phosphorylation of AMPK in LKB1-deficient cells that can be stimulated by Ca2+ ionophores, and studies using the CaMKK inhibitor STO-609 and isoform-specific siRNAs show that CaMKKbeta is required for this effect. CaMKKbeta also activates AMPK much more rapidly than CaMKKalpha in cell-free assays. K(+)-induced depolarization in rat cerebrocortical slices, which increases intracellular Ca2+ without disturbing cellular adenine nucleotide levels, activates AMPK, and this is blocked by STO-609. Our results suggest a potential Ca(2+)-dependent neuroprotective pathway involving phosphorylation and activation of AMPK by CaMKKbeta.

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Van Proeyen, K., De Bock, K., & Hespel, P. (2011) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1753-7 · Cited by 24
Research Progress on the Mechanism of Milk Fat Synthesis in Cows and the Effect of Conjugated Linoleic Acid on Milk Fat Metabolism and Its Underlying Mechanism: A Review
Guo, Y. X., Wei, Z., Zhang, Y., & Cao, J. (2024) · Animals · doi:10.3390/ani14020204 · Cited by 27
Regulation of autophagy by perilysosomal calcium: a new player in β-cell lipotoxicity
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LKB1 and AMPKα1 are required in pancreatic alpha cells for the normal regulation of glucagon secretion and responses to hypoglycemia
Sun, G., Xavier, G. D. S., Gorman, T., Priest, C., Solomou, A., Hodson, D. J., Foretz, M., Viollet, B., Herrera, P. L., Parker, H., et al. (2015) · Molecular Metabolism · doi:10.1016/j.molmet.2015.01.006 · Cited by 24
Mesenchymal Stromal Cells Accelerate Epithelial Tight Junction Assembly via the AMP-Activated Protein Kinase Pathway, Independently of Liver Kinase B1
Rowart, P., Erpicum, P., Krzesinski, J.-M., Sebbagh, M., & Jouret, F. (2017) · Stem Cells International · doi:10.1155/2017/9717353 · Cited by 24
Kaempferol improves glucose uptake in skeletal muscle via an AMPK-dependent mechanism
Moore, W. T., Luo, J., & Liu, D. (2023) · Food Science and Human Wellness · doi:10.1016/j.fshw.2023.03.028 · Cited by 26
TBC1D23 mediates Golgi-specific LKB1 signaling
Tu, Y., Yang, Q., Tang, M., Gao, L. P., Wang, Y., Wang, J., Liu, Z., Li, X., Mao, L., Jia, R. Z., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46166-2 · Cited by 28
Down‐regulation of calcium/calmodulin‐dependent protein kinase kinase 2 by androgen deprivation induces castration‐resistant prostate cancer
Shima, T., Mizokami, A., Miyagi, T., Kawai, K., Izumi, K., Kumaki, M., Ofude, M., Zhang, J., Keller, E. T., & Namiki, M. (2012) · The Prostate · doi:10.1002/pros.22533 · Cited by 24
Targeted Therapies of the LKB1/AMPK Pathway for the Treatment of Insulin Resistance
Yamada, E., Lee, T.-W. A., Pessin, J. E., & Bastie, C. C. (2010) · Future Medicinal Chemistry · doi:10.4155/fmc.10.264 · Cited by 25
Differential AMPK phosphorylation sites associated with phenylephrine vs. antihypertrophic effects of adenosine agonists in neonatal rat ventricular myocytes
Pang, T., Rajapurohitam, V., Cook, M. A., & Karmazyn, M. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00424.2009 · Cited by 24
Mice lacking AMP-activated protein kinase α1 catalytic subunit have increased bone remodelling and modified skeletal responses to hormonal challenges induced by ovariectomy and intermittent PTH treatment
Jeyabalan, J., Shah, M., Viollet, B., Roux, J. P., Chavassieux, P., Korbonits, M., & Chenu, C. (2012) · Journal of Endocrinology · doi:10.1530/joe-12-0184 · Cited by 24
Phosphodiesterase 4 inhibitor activates AMPK-SIRT6 pathway to prevent aging-related adipose deposition induced by metabolic disorder
Wang, Z., Liang, Y., Zhang, L., Zhang, N., Liu, Q., & Wang, Z. (2018) · Aging · doi:10.18632/aging.101559 · Cited by 24
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Li, M. H., Chen, W., Wang, L., Sun, J. L., Zhou, L., Shi, Y., Wang, C. H., Zhong, B. H., Shi, W. G., & Guo, Z. (2019) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.118.255216 · Cited by 24
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Williams, J. N., & Sankar, U. (2019) · Current Osteoporosis Reports · doi:10.1007/s11914-019-00518-w · Cited by 24
CDC25B partners with PP2A to induce AMPK activation and tumor suppression in triple negative breast cancer
Cairns, J., Ly, R. C., Niu, N., Kalari, K. R., Carlson, E. E., & Wang, L. (2020) · NAR Cancer · doi:10.1093/narcan/zcaa039 · Cited by 24
The role of AMPK in regulation of Na+,K+-ATPase in skeletal muscle: does the gauge always plug the sink?
Pirkmajer, S., Petrič, M., & Chibalin, A. (2021) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-020-09594-3 · Cited by 24
Absence of humoral mediated 5′AMP‐activated protein kinase activation in human skeletal muscle and adipose tissue during exercise
Kristensen, J. M., Johnsen, A., Birk, J. B., Nielsen, J. N., Jensen, B. R., Hellsten, Y., Richter, E. A., & Wojtaszewski, J. F. P. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.143123 · Cited by 24
Calcium signaling recruits substrate transporters GLUT4 and CD36 to the sarcolemma without increasing cardiac substrate uptake
Angın, Y., Schwenk, R. W., Nergiz‐Unal, R., Hoebers, N., Heemskerk, J. W. M., Kuijpers, M. J. E., Coumans, W. A., van Zandvoort, M. A. M. J., Bonen, A., Neumann, D., et al. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00655.2013 · Cited by 24
AMP‐activated protein kinase (AMPK)–dependent and –independent pathways regulate hypoxic inhibition of transepithelial Na+ transport across human airway epithelial cells
Cd, T., Smolenski, R. T., Harhun, M. I., Patel, H. S., Ahmed, S., Wanisch, K., Yáñez‐Muñoz, R. J., & Baines, D. L. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.01993.x · Cited by 24
Metabolic and transcriptome responses of RNAi-mediated AMPKα knockdown in Tribolium castaneum
Jiang, H., Zhang, N., Ji, C., Meng, X., Qian, K., Zheng, Y., & Wang, J. (2020) · BMC Genomics · doi:10.1186/s12864-020-07070-3 · Cited by 23
Dietary restriction to optimize T cell immunity is an ancient survival strategy conserved in vertebrate evolution
Li, K., Wei, X., Li, K., Zhang, Q., Zhang, J., Wang, D., & Yang, J. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04865-x · Cited by 23
Calcium signals tune AMPK activity and mitochondrial homeostasis in dendrites of developing neurons
Hatsuda, A., Kurisu, J., Fujishima, K., Kawaguchi, A., Ohno, N., & Kengaku, M. (2023) · Development · doi:10.1242/dev.201930 · Cited by 25
A Novel AMPK Inhibitor Sensitizes Pancreatic Cancer Cells to Ferroptosis Induction
Schneider, C., Hilbert, J., Génevaux, F., Höfer, S., Krauß, L., Schicktanz, F., Contreras, C. T., Jansari, S., Papargyriou, A., Richter, T., et al. (2024) · Advanced Science · doi:10.1002/advs.202307695 · Cited by 24
New insights into transduction pathways that regulate boar sperm function
de Llera, A. H., Martín‐Hidalgo, D., Gil, M. C., Garcı́a, L. J., & Bragado, M. J. (2015) · Theriogenology · doi:10.1016/j.theriogenology.2015.05.008 · Cited by 23
Enhanced activation of NAD(P)H
Kim, Y., Hwang, J. H., Kim, K.-S., Noh, J., Gang, G., Oh, W. K., Jeong, K., Kwak, T. H., Choi, H., Lee, I., et al. (2013) · Journal of Hypertension · doi:10.1097/hjh.0000000000000018 · Cited by 23
Role of the AMPK signaling pathway in early brain injury after subarachnoid hemorrhage in rats
An, J., Zhou, L., Sun, P., Pang, H., Li, Y., Yu, L., Zhang, M., & Song, J. (2015) · Acta Neurochirurgica · doi:10.1007/s00701-015-2370-3 · Cited by 23
Fish oil promotes survival and protects against cognitive decline in severely undernourished mice by normalizing satiety signals
Avraham, Y., Saidian, M., Burston, J. J., Mevorach, R., Vorobiev, L., Magen, I., Kunkes, E., Borges, B. C., Lichtman, A. H., & Berry, E. M. (2010) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2010.07.001 · Cited by 23
Clinical Relevance of Liver Kinase B1(LKB1) Protein and Gene Expression in Breast Cancer
Chen, I., Chang, Y., Lu, Y., Chung, K., Huang, C., Lu, T., Kuo, W., Wang, M., Kuo, K., Wu, P., et al. (2016) · Scientific Reports · doi:10.1038/srep21374 · Cited by 23
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Yi, Y., Gao, L., Wu, M. C., Ao, J., Zhang, C., Wang, X., Lin, M. T., Bergholz, J. S., Zhang, Y., & Xiao, Z. J. (2017) · Journal of Cancer · doi:10.7150/jca.19873 · Cited by 23
The red pepper’s spicy ingredient capsaicin activates AMPK in HepG2 cells through CaMKKβ
Bort, A., Sánchez, B. G., Spínola-Lasso, E., Mateos‐Gómez, P. A., Rodríguez‐Henche, N., & Díaz‐Laviada, I. (2019) · PLoS ONE · doi:10.1371/journal.pone.0211420 · Cited by 23

Authors: Hawley, S. A., Pan, D. A., Mustard, K. J., Ross, L., Bain, J., Edelman, A. M., Frenguelli, B. G., & Hardie, D. G.
Affiliations: University of Dundee (GB)
University at Buffalo, State University of New York (US)
Corresponding author: Hardie, D. Grahame
ORCID: Pan, David A.
Frenguelli, Bruno G.
Hardie, D. Grahame
Venue: Cell Metabolism
Publisher: Elsevier BV
Published: 2005-07
Volume: 2
Issue: 1
Pages: 9-19
ISSN: 1550-4131 (ISSN-L)
DOI: 10.1016/j.cmet.2005.05.009
OpenAlex: W2067979493
Cited by: 1,589
References: 48
Citations by year: 2026: 41 · 2025: 38 · 2024: 57 · 2023: 53 · 2022: 64 · 2021: 78 · 2020: 90 · 2019: 64 · 2018: 84 · 2017: 82 · 2016: 84 · 2015: 92 · 2014: 77 · 2013: 84 · 2012: 118
FWCI: 27.73
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2974 d)
Locations: Cell Metabolism (publishedVersion)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (submittedVersion)
Funders: Wellcome Trust
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Keywords: AMPK, CaMKKβ, LKB1, AMPK activation, upstream kinases, calcium ionophore, STO-609, potassium depolarization, intracellular calcium, neuroprotection, energy metabolism
MeSH terms: Calcimycin, Acetyl-CoA Carboxylase, Adenosine Diphosphate, Adenosine Triphosphate, Animals, Benzimidazoles, Brain, Enzyme Activation, Fibroblasts, HeLa Cells, Humans, Isoquinolines, Multienzyme Complexes, Phosphoprotein Phosphatases, Phosphorylation, Substrate Specificity, Protein Serine-Threonine Kinases, RNA, Small Interfering, Mice, Rats, Naphthalimides, Calcium-Calmodulin-Dependent Protein Kinase Kinase, AMP-Activated Protein Kinases, In Vitro Techniques

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Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase

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