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J. Biol. Chem., Vol. 279, Issue 34, 35176-35182, August 20, 2004

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The Muscle-specific Calmodulin-dependent Protein Kinase Assembles with the Glycolytic Enzyme Complex at the Sarcoplasmic Reticulum and Modulates the Activity of Glyceraldehyde-3-phosphate Dehydrogenase in a Ca²+/Calmodulin-dependent Manner^*

Puneet Singh, Maysoon Salih, John J. Leddy, and Balwant S. Tuana

From the Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, Ontario K1H 8M5, Canada

The skeletal muscle specific Ca²+/calmodulin-dependent protein kinase (CaMKII_M) is localized to the sarcoplasmic reticulum (SR) by an anchoring protein, KAP, but its function remains to be defined. Protein interactions of CaMKII_M indicated that it exists in complex with enzymes involved in glycolysis at the SR membrane. The kinase was found to complex with glycogen phosphorylase, glycogen debranching enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and creatine kinase in the SR membrane. CaMKII_M was also found to assemble with aldolase A, GAPDH, enolase, lactate dehydrogenase, creatine kinase, pyruvate kinase, and phosphorylase b kinase from the cytosolic fraction. The interacting proteins were substrates of CaMKII_M, and their phosphorylation was enhanced in a Ca²⁺- and calmodulin (CaM)-dependent manner. The CaMKII_M could directly phosphorylate GAPDH and markedly increase (3.4-fold) its activity in a Ca²⁺/CaM-dependent manner. These data suggest that the muscle CaMKII_M isoform may serve to assemble the glycogen-mobilizing and glycolytic enzymes at the SR membrane and specifically modulate the activity of GAPDH in response to calcium signaling. Thus, the activation of CaMKII_M in response to calcium signaling would serve to modulate GAPDH and thereby ATP and NADH levels at the SR membrane, which in turn will regulate calcium transport processes.

Received for publication, March 1, 2004 , and in revised form, May 24, 2004.

^* This work was supported by Grant 9596 from the Canadian Institute of Health Research (to B. S. T.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Cellular and Molecular Medicine, 451 Smyth Rd., University of Ottawa, Ottawa, Ontario K1H 8M5, Canada. Tel.: 613-562-5800 (ext. 8578); Fax: 613-562-5434; E-mail: btuana{at}uottawa.ca.

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