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J Biol Chem, Vol. 274, Issue 30, 20949-20952, July 23, 1999

Inhibitor-1 Is Not Required for the Activation of Glycogen Synthase by Insulin in Skeletal Muscle

Angus G. Scrimgeour, Patrick B. Allen^§, Allen A. Fienberg^§, Paul Greengard^§, and John C. Lawrence Jr.^¶

From the Departments of  Pharmacology and ^¶ Medicine, University of Virginia School of Medicine, Charlottesville, Virginia 22908 and the ^§ Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, New York, New York 10021-6399

Glycogen synthase is an excellent in vitro substrate for protein phosphatase-1 (PP1), which is potently inhibited by the phosphorylated forms of DARPP-32 (dopamine- and cAMP-regulated phosphoprotein, M_r = 32,000) and Inhibitor-1. To test the hypothesis that the activation of glycogen synthase by insulin is due to a decrease in the inhibition of PP1 by the phosphatase inhibitors, we have investigated the effects of insulin on glycogen synthesis in skeletal muscles from wild-type mice and mice lacking Inhibitor-1 and DARPP-32 as a result of targeted disruption of the genes encoding the two proteins. Insulin increased glycogen synthase activity and the synthesis of glycogen to the same extent in wild-type and knockout mice, indicating that neither Inhibitor-1 nor DARPP-32 is required for the full stimulatory effects of insulin on glycogen synthase and glycogen synthesis in skeletal muscle.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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