The substrate and sequence specificity of the AMP-activated protein kinase. Phosphorylation of glycogen synthase and phosphorylase kinase
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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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)
- ORCID
- Carling, David
- 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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