Details

Autor(en) / Beteiligte

• Cieniewski-Bernard, Caroline
• Lambert, Matthias
• Dupont, Erwan
• Montel, Valérie
• Stevens, Laurence
• Bastide, Bruno

Titel

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

Ist Teil von

• Frontiers in physiology, 2014, Vol.5, p.421-421

Ort / Verlag

Switzerland: Frontiers

Erscheinungsjahr

2014

Link zum Volltext

Quelle

Free E-Journal (出版社公開部分のみ）

Beschreibungen/Notizen

• 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.