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O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle
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 resistan...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4214218/ https://www.ncbi.nlm.nih.gov/pubmed/25400587 http://dx.doi.org/10.3389/fphys.2014.00421 |
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author | Cieniewski-Bernard, Caroline Lambert, Matthias Dupont, Erwan Montel, Valérie Stevens, Laurence Bastide, Bruno |
author_facet | Cieniewski-Bernard, Caroline Lambert, Matthias Dupont, Erwan Montel, Valérie Stevens, Laurence Bastide, Bruno |
author_sort | Cieniewski-Bernard, Caroline |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4214218 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-42142182014-11-14 O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle Cieniewski-Bernard, Caroline Lambert, Matthias Dupont, Erwan Montel, Valérie Stevens, Laurence Bastide, Bruno Front Physiol Physiology 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. Frontiers Media S.A. 2014-10-30 /pmc/articles/PMC4214218/ /pubmed/25400587 http://dx.doi.org/10.3389/fphys.2014.00421 Text en Copyright © 2014 Cieniewski-Bernard, Lambert, Dupont, Montel, Stevens and Bastide. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Physiology Cieniewski-Bernard, Caroline Lambert, Matthias Dupont, Erwan Montel, Valérie Stevens, Laurence Bastide, Bruno O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle |
title | O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle |
title_full | O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle |
title_fullStr | O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle |
title_full_unstemmed | O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle |
title_short | O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle |
title_sort | o-glcnacylation, contractile protein modifications and calcium affinity in skeletal muscle |
topic | Physiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4214218/ https://www.ncbi.nlm.nih.gov/pubmed/25400587 http://dx.doi.org/10.3389/fphys.2014.00421 |
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