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CELL GROWTH AND DEVELOPMENT

Glycogen Synthase Kinase 3 Is an Insulin-Regulated C/EBPα Kinase

Sarah E. Ross, Robin L. Erickson, Nahid Hemati, Ormond A. MacDougald
Sarah E. Ross
Department of Physiology, University of Michigan Medical School, Ann Arbor, MI 48109-0622
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Robin L. Erickson
Department of Physiology, University of Michigan Medical School, Ann Arbor, MI 48109-0622
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Nahid Hemati
Department of Physiology, University of Michigan Medical School, Ann Arbor, MI 48109-0622
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Ormond A. MacDougald
Department of Physiology, University of Michigan Medical School, Ann Arbor, MI 48109-0622
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DOI: 10.1128/MCB.19.12.8433
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ABSTRACT

CCAAT/enhancer binding protein α (C/EBPα) is a transcription factor involved in creating and maintaining the adipocyte phenotype. We have shown previously that insulin stimulates dephosphorylation of C/EBPα in 3T3-L1 adipocytes. Studies to identify the insulin-sensitive sites of phosphorylation reveal that a C/EBPα peptide (amino acids H215 to K250) is phosphorylated on T222, T226, and S230 in vivo. The context of these phosphoamino acids implicates glycogen synthase kinase 3 (GSK3), whose activity is known to be repressed in response to insulin, as a potential kinase for phosphorylation of T222 and T226. Accordingly, GSK3 phosphorylates the predicted region of C/EBPα on threonine in vitro, and GSK3 uses C/EBPα as a substrate in vivo. In addition, the effect of pharmacological agents on GSK3 activity correlates with regulation of C/EBPα phosphorylation. Treatment of 3T3-L1 adipocytes with the phosphatidylinositol 3-kinase inhibitor wortmannin results in phosphorylation of C/EBPα, whereas treatment with the GSK3 inhibitor lithium results in dephosphorylation of C/EBPα. Collectively, these data indicate that insulin stimulates dephosphorylation of C/EBPα on T222 and T226 through inactivation of GSK3. Since dephosphorylation of C/EBPα in response to lithium is blocked by okadaic acid, strong candidates for the T222 and T226 phosphatase are protein phosphatases 1 and 2a. Treatment of adipocytes with insulin alters the protease accessibility of widespread sites within the N terminus of C/EBPα, consistent with phosphorylation causing profound conformational changes. Finally, phosphorylation of C/EBPα and other substrates by GSK3 may be required for adipogenesis, since treatment of differentiating preadipocytes with lithium inhibits their conversion to adipocytes.

  • Copyright © 1999 American Society for Microbiology
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Glycogen Synthase Kinase 3 Is an Insulin-Regulated C/EBPα Kinase
Sarah E. Ross, Robin L. Erickson, Nahid Hemati, Ormond A. MacDougald
Molecular and Cellular Biology Dec 1999, 19 (12) 8433-8441; DOI: 10.1128/MCB.19.12.8433

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Glycogen Synthase Kinase 3 Is an Insulin-Regulated C/EBPα Kinase
Sarah E. Ross, Robin L. Erickson, Nahid Hemati, Ormond A. MacDougald
Molecular and Cellular Biology Dec 1999, 19 (12) 8433-8441; DOI: 10.1128/MCB.19.12.8433
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KEYWORDS

Calcium-Calmodulin-Dependent Protein Kinases
DNA-Binding Proteins
insulin
Nuclear Proteins
transcription factors

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