Cited by 296Metabolism, Diabetes, and CancerProtein Kinase Regulation and GTPase SignalingGlycogen Storage Diseases and Myoclonus

The substrate and sequence specificity of the AMP-activated protein kinase. Phosphorylation of glycogen synthase and phosphorylase kinase

Carling, David, Grahame Hardie, D.·1989·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Abstract

In addition to acetyl-CoA carboxylase and HMG-CoA reductase, the AMP-activated protein kinase phosphorylates glycogen synthase, phosphorylase kinase, hormone-sensitive lipase and casein. A number of other substrates for the cyclic AMP-dependent protein kinase, e.g., L-pyruvate kinase and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, are not phosphorylated at significant rates. Examination of the sites phosphorylated on acetyl-CoA carboxylase, hormone-sensitive lipase, glycogen synthase and phosphorylase kinase suggests a consensus recognition sequence in which the serine residue phosphorylated by the AMP-activated protein kinase has a hydrophobic residue on the N-terminal side (i.e., at -1) and at least one arginine residue at -2, -3 or -4. Substrates for cyclic AMP-dependent protein kinase which lack the hydrophobic residue at -1 are not substrates for the AMP-activated protein kinase.

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Crossref · 10.1016/0167-4889(89)90014-1

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  • AMPK regulates glycogen synthesis through phosphorylation of glycogen synthase (GS) at site 2 (S7).

    “AMPK regulates glycogen synthesis through phosphorylation of glycogen synthase (GS) at site 2 (S7) [132].”

    From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [132]

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Authors
Carling, D., & Grahame Hardie, D.
Affiliations
University of Dundee (GB)
Venue
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher
Elsevier BV
Published
1989-06
Volume
1012
Issue
1
Pages
81-86
ISSN
0167-4889 (ISSN-L)
OpenAlex
W2157804459
Cited by
296
References
24
Citations by year
2025: 3 · 2024: 2 · 2023: 4 · 2022: 8 · 2021: 3 · 2020: 8 · 2019: 4 · 2018: 11 · 2017: 7 · 2016: 7 · 2015: 25 · 2014: 11 · 2013: 15 · 2012: 19
FWCI
0.90
Type
journal article
Language
en
Open access
closed
Locations
  • Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
  • PubMed (publishedVersion)
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
  • Health Sciences › Medicine › Rheumatology › Glycogen Storage Diseases and Myoclonus
Keywords
AMPK, substrate specificity, phosphorylation sites, glycogen synthase, phosphorylase kinase, hormone-sensitive lipase, acetyl-CoA carboxylase, protein kinase A, serine phosphorylation, arginine residues
MeSH terms
Acetyl-CoA Carboxylase, Cyclic AMP, Adenosine Monophosphate, Amino Acid Sequence, Animals, Caseins, Cattle, Enzyme Activation, Glycogen Synthase, Hydroxymethylglutaryl CoA Reductases, Kinetics, Lipase, Molecular Sequence Data, Phosphorylase Kinase, Phosphorylation, Protein Kinases, Rabbits, Substrate Specificity, Rats

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