Cited by 353Metabolism, Diabetes, and CancerPI3K/AKT/mTOR signaling in cancerRNA and protein synthesis mechanisms

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Stimulation of the AMP-activated Protein Kinase Leads to Activation of Eukaryotic Elongation Factor 2 Kinase and to Its Phosphorylation at a Novel Site, Serine 398

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Browne, Gareth J., Finn, Stephen G., Proud, Christopher G.·2004·Journal of Biological Chemistry

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Abstract

Protein synthesis consumes a high proportion of the metabolic energy of mammalian cells, and most of this is used by peptide chain elongation. An important regulator of energy supply and demand in eukaryotic cells is the AMP-activated protein kinase (AMPK). The rate of peptide chain elongation can be modulated through the phosphorylation of eukaryotic elongation factor (eEF) 2, which inhibits its activity and is catalyzed by a specific calcium/calmodulin-dependent protein kinase termed eEF2 kinase. Here we show that AMPK directly phosphorylates eEF2 kinase, and we identify the major site of phosphorylation as Ser-398 in a regulatory domain of eEF2 kinase. AMPK also phosphorylates two other sites (Ser-78 and Ser-366) in eEF2 kinase in vitro. We develop appropriate phosphospecific antisera and show that phosphorylation of Ser-398 in eEF2 kinase is enhanced in intact cells under a range of conditions that activate AMPK and increase the phosphorylation of eEF2. Ser-78 and Ser-366 do not appear to be phosphorylated by AMPK within cells. Although cardiomyocytes appear to contain a distinct isoform of eEF2 kinase, it also contains a site corresponding to Ser-398 that is phosphorylated by AMPK in vitro. Stimuli that activate AMPK and increase eEF2 phosphorylation within cells increase the activity of eEF2 kinase. Thus, AMPK and eEF2 kinase may provide a key link between cellular energy status and the inhibition of protein synthesis, a major consumer of metabolic energy.

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Authors: Browne, G. J., Finn, S. G., & Proud, C. G.
Affiliations: University of Dundee (GB)
Corresponding author: Proud, Christopher G.
ORCID: Browne, Gareth J.
Proud, Christopher G.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2004-03
Volume: 279
Issue: 13
Pages: 12220-12231
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m309773200
OpenAlex: W1983195734
Cited by: 353
References: 35
Citations by year: 2026: 8 · 2025: 8 · 2024: 7 · 2023: 11 · 2022: 7 · 2021: 15 · 2020: 16 · 2019: 9 · 2018: 11 · 2017: 16 · 2016: 18 · 2015: 20 · 2014: 19 · 2013: 20 · 2012: 25
FWCI: 7.82
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6057 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
ePrints Soton (University of Southampton) (submittedVersion)
Funders: British Heart Foundation
Directorate for Biological Sciences
Biotechnology and Biological Sciences Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords: AMPK, eEF2K, eEF2 kinase, eEF2 phosphorylation, translation elongation, protein synthesis regulation, cellular energy status, cardiomyocytes
MeSH terms: Amino Acid Sequence, Animals, Binding Sites, Cells, Cultured, Enzyme Activation, Glutathione Transferase, Humans, Molecular Sequence Data, Multienzyme Complexes, Peptides, Phosphorylation, Precipitin Tests, Serine, Time Factors, Immunoblotting, Blotting, Western, Mutagenesis, Protein Serine-Threonine Kinases, Protein Structure, Tertiary, Calcium-Calmodulin-Dependent Protein Kinases, DNA, Complementary, Protein Isoforms, Myocytes, Cardiac, Rats, Elongation Factor 2 Kinase, AMP-Activated Protein Kinases

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Stimulation of the AMP-activated Protein Kinase Leads to Activation of Eukaryotic Elongation Factor 2 Kinase and to Its Phosphorylation at a Novel Site, Serine 398

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