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Article Dans Une Revue Proceedings of the Nutrition Society Année : 2004

The role of ubiquitin–proteasome-dependent proteolysis in the remodelling of skeletal muscle

Daniel Taillandier
Lydie Combaret
Marie-Noëlle Pouch
  • Fonction : Auteur
Susan Samuels
  • Fonction : Auteur
Daniel Bechet

Résumé

In skeletal muscle, as in any mammalian tissue, protein levels are dictated by relative rates of protein synthesis and breakdown. Recent studies have shown that the ubiquitin-proteasome-dependent proteolytic pathway is mainly responsible for the breakdown of myofibrillar proteins. In this pathway proteins that are to be degraded are first tagged with a polyubiquitin degradation signal. Ubiquitination is performed by the ubiquitin-activating enzyme, ubiquitin-conjugating enzymes and ubiquitin-protein ligases, which are responsible for the recognition of specific substrates. Polyubiquitinated protein substrates are then specifically recognised and degraded by the 26S proteasome. The present review focuses on: (1) the mechanisms of ubiquitination-deubiquitination that make the system highly selective; (2) the mechanisms of proteolysis in skeletal muscle. In particular, the role of the system in the remodelling of skeletal muscle during exercise and disuse and in recovery or regeneration that prevails during post-atrophic conditions is reviewed.
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Dates et versions

hal-01919672 , version 1 (12-11-2018)

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Daniel Taillandier, Lydie Combaret, Marie-Noëlle Pouch, Susan Samuels, Daniel Bechet, et al.. The role of ubiquitin–proteasome-dependent proteolysis in the remodelling of skeletal muscle. Proceedings of the Nutrition Society, 2004, 63 (2), pp.357 - 361. ⟨10.1079/PAR2004358⟩. ⟨hal-01919672⟩
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