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J. Biol. Chem., Vol. 282, Issue 14, 10360-10369, April 6, 2007

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O-Linked N-Acetylglucosaminylation Is Involved in the Ca²⁺ Activation Properties of Rat Skeletal Muscle^*

Julie Hedou¹², Caroline Cieniewski-Bernard²³, Yves Leroy, Jean-Claude Michalski, Yvonne Mounier, and Bruno Bastide⁴

From the Laboratoire de Plasticité Neuromusculaire, Unité de Neurosciences et Physiologie Adaptatives, UPRES EA 4052 and Unité Mixte de Recherche CNRS 8576 "Glycobiologie Structurale et Fonctionnelle," IFR118, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France

O-Linked N-acetylglucosaminylation termed O-GlcNAc is a dynamic cytosolic and nuclear glycosylation that is dependent both on glucose flow through the hexosamine biosynthesis pathway and on phosphorylation because of the existence of a balance between phosphorylation and O-GlcNAc. This glycosylation is a ubiquitous post-translational modification, which probably plays an important role in many aspects of protein functions. We have previously reported that, in skeletal muscle, proteins of the glycolytic pathway, energetic metabolism, and contractile proteins were O-GlcNAc-modified and that O-Glc-NAc variations could control the muscle protein homeostasis and be implicated in the regulation of muscular atrophy.

In this paper, we report O-N-acetylglucosaminylation of a number of key contractile proteins (i.e. myosin heavy and light chains and actin), which suggests that this glycosylation could be involved in skeletal muscle contraction. Moreover, our results showed that incubation of skeletal muscle skinned fibers in N-acetyl-D-glucosamine, in a concentration solution known to inhibit O-GlcNAc-dependent interactions, induced a decrease in calcium sensitivity and affinity of muscular fibers, whereas the cooperativity of the thin filament proteins was not modified. Thus, our results suggest that O-GlcNAc is involved in contractile protein interactions and could thereby modulate muscle contraction.

Received for publication, July 17, 2006 , and in revised form, December 19, 2006.

^* This work was supported by CNRS/Unité Mixte de Recherche 8576 and Centre National d'Etudes Spatiales (CNES) Grant 3194-2002. 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.

¹ Recipient of a fellowship from the CNES and the region Nord Pas de Calais.

² These two authors contributed equally to this work.

³ Recipient of a fellowship from the Fondation pour la Recherche Médicale.

⁴ To whom correspondence should be addressed: Laboratoire de Neurosciences et Physiologie Adaptatives, EA 4052, UFR Biologie, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France. Tel.: 33-3204340; Fax: 33-320436888; E-mail: bruno.bastide{at}univ-lille1.fr.

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