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Originally published In Press as doi:10.1074/jbc.M909303199 on March 15, 2000

J. Biol. Chem., Vol. 275, Issue 21, 15940-15947, May 26, 2000
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Insulin-stimulated Phosphorylation of the Protein Phosphatase-1 Striated Muscle Glycogen-targeting Subunit and Activation of Glycogen Synthase*

Jun LiuDagger and David L. Brautigan§

From the Center for Cell Signaling, University of Virginia School of Medicine, Charlottesville, Virginia 22908

Protein phosphatase-1 (PP-1) in heart and skeletal muscle binds to a glycogen-targeting subunit (GM) in the sarcoplasmic reticulum. Phosphorylation of GM has been postulated to govern activity of PP1 in response to adrenaline and insulin. In this study, we used biochemical assays and GM expression in living cells to examine the effects of insulin on the phosphorylation of GM, and the binding of PP-1 to GM. We also assayed glycogen synthase activation in cells expressing wild type GM and GM mutated at the phosphorylation sites. In biochemical assays kinase(s) prepared from insulin-stimulated Chinese hamster ovary (CHO-IR) cells and C2C12 myotubes phosphorylated a glutathione S-transferase (GST) fusion protein, GST-GM(1-240), at both site 1 (Ser48) and site 2 (Ser67). Phosphorylation of both sites was dependent on activation of the mitogen-activated protein kinase pathway, involving in particular ribosomal protein S6 kinase. Full-length GM was expressed in CHO-IR cells and metabolic 32P labeling at sites 1 and 2 was increased by insulin treatment. The GM expressed in CHO-IR cells or in C2C12 myotubes co-immunoprecipitated endogenous PP-1, and association was transiently lost following treatment of the cells with insulin. In contrast PP-1 binding to GM(S67T), a version of GM not phosphorylated at site 2, was unaffected by insulin treatment. Expression of GM increased basal activity of endogenous glycogen synthase in CHO-IR cells. Insulin stimulated glycogen synthase activity the same extent in cells expressing wild type GM or GM mutated to eliminate phosphorylation site 1 and/or site 2. Phosphorylation of GM is stimulated by insulin, but this phosphorylation is not involved in insulin control of glycogen metabolism. We speculate that other functions of GM at the sarcoplasmic reticulum membrane might be affected by insulin.

* This work was supported in part by National Institutes of Health Grants CA77584 and GM56362 (to D. L. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by the Molecular Medicine Program made possible by a grant from the Lucille P. Markey Charitable Trust.

§ To whom correspondence should be addressed: Center for Cell Signaling, University of Virginia School of Medicine, P. O. Box 800577, West Complex 7196, Charlottesville, VA 22908-0577. Tel.: 804-924-5892; Fax: 804-243-2829; E-mail: db8g@virginia.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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