A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis

Carling, David; Zammit, Victor A.; Hardie, D.Grahame

doi:10.1016/0014-5793(87)80292-2

Cited by 599Cancer, Lipids, and MetabolismLipid metabolism and biosynthesisCholesterol and Lipid Metabolism

A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis

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Carling, David, Zammit, Victor A., Hardie, D.Grahame·1987·FEBS Letters

DOI 10.1016/0014-5793(87)80292-2

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Abstract

A highly purified rat liver protein kinase phosphorylates and inactivates acetyl-CoA carboxylase, and causes rapid inactivation of microsomal HMG-CoA reductase in the presence of MgATP. Both effects are stimulated in an identical manner by AMP, and are greatly reduced by prior treatment of the kinase with purified protein phosphatase. The dephosphorylated kinase can be reactivated in the presence of MgATP, apparently due to a distinct kinase kinase, and this reactivation is stimulated by nanomolar concentrations of palmitoyl-CoA. These results show that a common, bicyclic protein kinase cascade can potently inactivate the regulatory enzymes of both fatty acid and cholesterol biosynthesis.

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Once activated, AMPK redirects metabolism toward increased catabolism or decreased anabolism through phosphorylation of key proteins across multiple pathways, including protein synthesis, lipid homeostasis, glucose metabolism, and mitochondrial homeostasis.
“Once activated, AMPK redirects metabolism toward increased catabolism or decreased anabolism through the phosphorylation of key proteins across multiple pathways, including protein synthesis (e.g., mammalian target of rapamycin complex (1) [2,3], lipid homeostasis (e.g., acetyl coenzyme A carboxylase, ACC) [4,5], glucose metabolism (e.g., phosphofructokinase (2) [6], and mitochondrial homeostasis”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [4]

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Molecular aspects of cellular regulation
Cohen, P. (1980) · Elsevier eBooks · Cited by 393 · see citing works
Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme
Gil, G., Faust, J. R., Chin, D. J., Goldstein, J. L., & Brown, M. S. (1985) · Cell · doi:10.1016/0092-8674(85)90078-9 · Cited by 386 · see citing works
In vivo demonstration of the circadian rhythm of cholesterol biosynthesis inthe liver and intestine of the rat
Edwards, P. A., Muroya, H., & Gould, R. G. (1972) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)39403-7 · Cited by 217 · see citing works
Regulation of synthesis and degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase by low density lipoprotein and 25-hydroxycholesterol in UT-1 cells.
Faust, J. R., Luskey, K. L., Chin, D. J., et al. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.17.5205 · Cited by 205 · see citing works
Reversible modulation of the activities of both liver microsomal hydroxymethylglutaryl coenzyme a reductase and its inactivating enzyme. Evidence for regulation by phosphorylation-dephosphorylation
Ingebritsen, T. S., Lee, H.-S., Parker, R. A., et al. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)91273-1 · Cited by 144 · see citing works
Modulation of hydroxymethylglutaryl-CoA reductase activity, reductase kinase activity, and cholesterol synthesis in rat hepatocytes in response to insulin and glucagon.
Ingebritsen, T. S., Geelen, M. J. H., Parker, R. A., Evenson, K. J., & Gibson, D. M. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86661-9 · Cited by 142 · see citing works
Effect of diet on activity of enzymes involved in fatty acid and cholesterol synthesis.
Romsos, D. R., & Leveille, G. A. (1974) · PubMed · Cited by 118 · see citing works
Activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl Coenzyme A reductase kinase by adenosine 5′-monophosphate
Ferrer, A., Caelles, C., Massot, N., & Hegardt, F. G. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(85)91161-1 · Cited by 118 · see citing works
Reversible Phosphorylation and Inactivation of Acetyl‐CoA Carboxylase from Lactating Rat Mammary Gland by Cyclic AMP‐Dependent Protein Kinase
Hardie, D. G., & Guy, P. S. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb04852.x · Cited by 111 · see citing works
Self-citation
Glucagon inhibits fatty acid synthesis in isolated hepatocytes via phosphorylation of acetyl-CoA carboxylase by cyclic-AMP-dependent protein kinase
Holland, R., Witters, L. A., & Hardie, D. G. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08105.x · Cited by 99 · see citing works
Self-citation
Effect of Diet on Activity of Enzymes Involved in Fatty Acid and Cholesterol Synthesis1 1Studies conducted by the authors were aided by Grants HE 13245, HL-14677, AM-10774, and AM-15847 from the National Institutes of Health, U. S. Public Health Service, Washington, D. C.
Romsos, D. R., & Leveille, G. A. (1974) · Advances in lipid research · doi:10.1016/b978-0-12-024912-1.50010-7 · Cited by 97 · see citing works
Characterization and regulation of reductase kinase, a protein kinase that modulates the enzymic activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Beg, Z. H., Stonik, J. A., & Brewer, H. B. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4375 · Cited by 76 · see citing works
The in vivo regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase. Phosphorylation of the enzyme as an early regulatory response following cholesterol feeding.
Arebalo, R. E., Hardgrave, J. E., & Scallen, T. J. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70008-8 · Cited by 67 · see citing works
Diurnal changes in the fraction of 3-hydroxy-3-methylglutaryl-CoA reductase in the active form in rat liver microsomal fractions
Easom, R. A., & Zammit, V. A. (1984) · Biochemical Journal · doi:10.1042/bj2200739 · Cited by 60 · see citing works
Self-citation
Isolation of three cyclic-AMP-independent acetyl-CoA carboxylase kinases from lactating rat mammary gland and characterization of their effects on enzyme activity
Munday, M. R., & Hardie, D. G. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08237.x · Cited by 43 · see citing works
Self-citation
Evidence that changes in hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase activity are required partly to maintain a constant rate of sterol synthesis.
Gibbons, G. F., Björnsson, O. G., & Pullinger, C. R. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42613-5 · Cited by 37 · see citing works
[55] 3-Hydroxy-3-methylglutaryl-CoA reductase from rat liver
Kleinsek, D. A., Dugan, R. E., Baker, T. A., et al. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(81)71057-7 · Cited by 33 · see citing works
Diurnal variations of lipogenic enzymes, their substrate and effector levels and lipogenesis from tritiated water in rat liver
Fukuda, H., Katsurada, A., & Iritani, N. (1985) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(85)90269-3 · Cited by 32 · see citing works
Characterization of the phosphorylation of rat mammary ATP‐citrate lyase and acetyl‐CoA carboxylase by Ca2+ and calmodulin‐dependent multiprotein kinase and Ca2+ and phospholipid‐dependent protein kinase
Hardie, D. G., Carling, D., Ferrari, S. M., et al. (1986) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1986.tb09702.x · Cited by 28 · see citing works
Self-citation
5 Acetyl-Coenzyme A Carboxylase
Brownsey, R. W., & Denton, R. M. (1987) · The Enzymes · doi:10.1016/s1874-6047(08)60256-5 · Cited by 26 · see citing works
Phosphorylation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase
Ferrer, A., & Hegardt, F. G. (1984) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(84)90104-8 · Cited by 21 · see citing works
7 Hydroxymethylglutaryl-Coenzyme A Reductase
Gibson, D. M., & Parker, R. A. (1987) · The Enzymes · doi:10.1016/s1874-6047(08)60258-9 · Cited by 16 · see citing works
The role of phosphorylation/dephosphorylation of acetyl-CoA carboxylase in the regulation of mammalian fatty acid biosynthesis
Munday, M. R., Haystead, T., Holland, R., et al. (1986) · Biochemical Society Transactions · doi:10.1042/bst0140559 · Cited by 11 · see citing works
Diurnal variations in the effects of an unsaturated-fat-containing diet on fatty acid and cholesterol synthesis in rat hepatocytes
Gibbons, G. F., & Pullinger, C. R. (1986) · Biochemical Journal · doi:10.1042/bj2390617 · Cited by 11 · see citing works
Isolation of a cyclic-AMP-independent protein kinase from rat liver and its effect on the enzymic activity of acetyl-CoA carboxylase
Carling, D., & Hardie, D. G. (1986) · Biochemical Society Transactions · doi:10.1042/bst0141076 · Cited by 11 · see citing works
Self-citation

Flagged first, then by citations

Research works printed but not linked: 6

Munday, M.R., Haystead, T.A. J., Holland, R., Carling, D. and Hardie, D.G. (1986) Biochem. Sot. Trans. 14, 559-562.
Brownsey, R.W. and Denton, R.M. (1987) in: The Enzymes (Boyer, P.D. and Krebs, E.G. eds) 3rd edn, ~01.18, pp.123-146, Academic Press, New York.
Carling, D. and Hardie, D.G. (1986) Biochem. Sot. Trans. 14, 1076-1077.
Gibson, D.M. and Parker, R.A. (1987) in: The Enzymes (Boyer, P.D. and Krebs, E.G. eds) 3rd edn, ~01.18, pp.179-215, Academic Press, New York.
Beg, Z.H., Stonik, J.A. and Brewer, H.B. (1979) Proc. Natl. Acad. Sci. USA 76, 4375-4379.
Faust, J.R., Luskey, K.L., Chin, D.J., Goldstein, J.L. and Brown, M.S. (1982) Proc. Natl. Acad. Sci. USA 79, 5205-5209.

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Shackelford, D. B., & Shaw, R. J. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2676 · Cited by 1,943 · see citing works
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Mitochondrial involvement in skeletal muscle insulin resistance: A case of imbalanced bioenergetics
Affourtit, C. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.07.008 · Cited by 67 · see citing works
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Chung, M.-M., Nicol, C. J., Cheng, Y.-C., Lin, K.-H., Chen, Y.-L., Pei, D., Lin, C.-H., Shih, Y.-N., Yen, C.-H., Chen, S.-J., et al. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.01.017 · Cited by 66 · see citing works
The physiology and pathophysiology of the neural control of the counterregulatory response
Beall, C., Ashford, M. L., & McCrimmon, R. J. (2012) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00531.2011 · Cited by 63 · see citing works
Insulin Regulation of Hepatic Lipid Homeostasis
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Mitochondrial and performance adaptations to exercise training in mice lacking skeletal muscle LKB1
Tanner, C. B., Madsen, S. R., Hallowell, D. M., Goring, D. M. J., Moore, T. M., Hardman, S. E., Heninger, M. R., Atwood, D. R., & Thomson, D. M. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00227.2013 · Cited by 47 · see citing works

Inhibition of Abscisic Acid Biosynthesis in Cercospora rosicola by Inhibitors of Gibberellin Biosynthesis and Plant Growth Retardants
Norman, S. M., Poling, S. M., Maier, V. P., et al. (1983) · PLANT PHYSIOLOGY · doi:10.1104/pp.71.1.15 · Cited by 29 · see citing works
[Studies on the semi-biosynthesis of L-ephedrine (I). Studies on the biosynthesis of L-phenyl acetyl carbinol].
Xu, X.-Y., Ym, Z., Sz, W., et al. (2001) · PubMed
Possible ways of fagopyrin biosynthesis and production in buckwheat plants
Sytar, O., Brestič, M., & Rai, M. (2012) · Fitoterapia · doi:10.1016/j.fitote.2012.10.008 · Cited by 17 · see citing works
Ornithine biosynthesis, and arginine biosynthesis and degradation in plant cells
Shargool, D., Jain, J. C., & McKay, G. (1988) · Phytochemistry · doi:10.1016/0031-9422(88)80404-7 · Cited by 80 · see citing works
ChemInform Abstract: BIOSYNTHESIS OF THE LINCOMYCINS. 1. STUDIES USING STABLE ISOTOPES ON THE BIOSYNTHESIS OF THE PROPYL‐ AND ETHYL‐L‐HYGRIC ACID MOIETIES OF LINCOMYCINS A AND B
Brahme, N. M., González, J. E., Rolls, J. P., et al. (1985) · ChemInform · doi:10.1002/chin.198515358

Authors: Carling, D., Zammit, V. A., & Hardie, D. G.
Affiliations: University of Dundee (GB)
Hannah Research Foundation (GB)
Corresponding author: Hardie, D.Grahame
ORCID: Carling, David
Zammit, Victor A.
Hardie, D.Grahame
Venue: FEBS Letters
Publisher: Wiley
Published: 1987-11-02
Volume: 223
Issue: 2
Pages: 217-222
ISSN: 0014-5793 (ISSN-L)
1873-3468
DOI: 10.1016/0014-5793(87)80292-2
OpenAlex: W2033823674
Cited by: 599
References: 25
Citations by year: 2026: 11 · 2025: 24 · 2024: 20 · 2023: 23 · 2022: 27 · 2021: 30 · 2020: 29 · 2019: 30 · 2018: 23 · 2017: 14 · 2016: 28 · 2015: 17 · 2014: 24 · 2013: 30 · 2012: 22
FWCI: 6.48
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 5100 d)
Locations: FEBS Letters (publishedVersion)
PubMed (publishedVersion)
Funders: British Heart Foundation
Medical Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
Keywords: protein kinase cascades, acetyl-CoA carboxylase, HMG-CoA reductase, fatty acid synthesis, cholesterol biosynthesis, AMP, palmitoyl-CoA, kinase dephosphorylation, protein phosphatase, enzyme inactivation
MeSH terms: Acetyl-CoA Carboxylase, Adenosine Monophosphate, Animals, Cholesterol, Fatty Acids, Hydroxymethylglutaryl CoA Reductases, Ligases, Liver, Phosphoprotein Phosphatases, Phosphoproteins, Phosphorylation, Protein Kinases, Rats

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A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis

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