The low activity of acetyl-CoA car☐ylase in basal and glucagon-stimulated hepatocytes is due to phosphorylation by the AMP-activated protein kinase and not cyclic AMP-dependent protein kinase-Reference-Cited by-同舟云学术

The low activity of acetyl-CoA car☐ylase in basal and glucagon-stimulated hepatocytes is due to phosphorylation by the AMP-activated protein kinase and not cyclic AMP-dependent protein kinase

Published:1988-06-20 Issue:2 Volume:233 Page:294-298
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Sim Alastair T.R.,Hardie D.G.

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(88)80445-9/fullpdf

Reference20 articles.

1. Hardie D.G. Cohen P. Molecular Aspects of Cellular Regulation 1 1980 Elsevier Amsterdam, New York 33 62

2. The role of phosphorylation/dephosphorylation of acetyl-CoA carboxylase in the regulation of mammalian fatty acid biosynthesis

3. Reversible Phosphorylation and Inactivation of Acetyl-CoA Carboxylase from Lactating Rat Mammary Gland by Cyclic AMP-Dependent Protein Kinase

4. In vitro phosphorylation and inactivation of rat liver acetyl-CoA carboxylase purified by avidin affinity chromatography

5. Isolation of a cyclic-AMP-independent protein kinase from rat liver and its effect on the enzymic activity of acetyl-CoA carboxylase

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