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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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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