Functional characterisation of the regulation of CAAT enhancer binding protein alpha by GSK-3 phosphorylation of Threonines 222/226 |
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| Authors: | H-K Liu S Perrier C Lipina D Finlay H McLauchlan CJ Hastie HS Hundal C Sutherland |
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| Institution: | (1) Division of Molecular Physiology, School of Life Sciences, University of Dundee, Dundee, DD1 4HN, UK;(2) Division of Pathology and Neurosciences, Ninewells Medical School, University of Dundee, Dundee, DD1 9SY, UK;(3) Division of Signal Transduction and Therapy, School of Life Sciences, University of Dundee, Dundee, DD1 4HN, UK;(4) National Research Institute of Chinese Medicine, Taipei, Taiwan, Republic of China |
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| Abstract: | Background Glycogen Synthase Kinase-3 (GSK3) activity is repressed following insulin treatment of cells. Pharmacological inhibition of
GSK3 mimics the effect of insulin on Phosphoenolpyruvate Carboxykinase (PEPCK), Glucose-6 Phosphatase (G6Pase) and IGF binding protein-1 (IGFBP1) gene expression. CAAT/enhancer
binding protein alpha (C/EBPα) regulates these gene promoters in liver and is phosphorylated on two residues (T222/T226) by
GSK3, although the functional outcome of the phosphorylation has not been established. We aimed to establish whether CEBPα
is a link between GSK3 and these gene promoters. |
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