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Review
. 2014 Oct 30:5:421.
doi: 10.3389/fphys.2014.00421. eCollection 2014.

O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle

Caroline Cieniewski-Bernard  1 , Matthias Lambert  1 , Erwan Dupont  1 , Valérie Montel  1 , Laurence Stevens  1 , Bruno Bastide  1
Affiliations
Review

O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle

Caroline Cieniewski-Bernard et al. Front Physiol. .

Abstract

O-GlcNAcylation, a generally undermined atypical protein glycosylation process, is involved in a dynamic and highly regulated interplay with phosphorylation. Akin to phosphorylation, O-GlcNAcylation is also involved in the physiopathology of several acquired diseases, such as muscle insulin resistance or muscle atrophy. Recent data underline that the interplay between phosphorylation and O-GlcNAcylation acts as a modulator of skeletal muscle contractile activity. In particular, the O-GlcNAcylation level of the phosphoprotein myosin light chain 2 seems to be crucial in the modulation of the calcium activation properties, and should be responsible for changes in calcium properties observed in functional atrophy. Moreover, since several key structural proteins are O-GlcNAc-modified, and because of the localization of the enzymes involved in the O-GlcNAcylation/de-O-GlcNAcylation process to the nodal Z disk, a role of O-GlcNAcylation in the modulation of the sarcomeric structure should be considered.

Keywords: MLC2; O-GlcNAcylation; O-GlcNAcylation/phosphorylation interplay; contractile properties; contractile proteins; phosphorylation; sarcomeric structure.

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Figures

Figure 1
Figure 1
Diagram showing various effects and implications of O-GlcNAcylation in skeletal muscle.
See this image and copyright information in PMC

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