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

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 pr...

Full description

Saved in:
Bibliographic Details
Published inProceedings of the Nutrition Society Vol. 63; no. 2; pp. 357 - 361
Main Authors Taillandier, Daniel, Combaret, Lydie, Pouch, Marie-Noëlle, Samuels, Susan E., Béchet, Daniel, Attaix, Didier
Format Journal Article
LanguageEnglish
Published Cambridge, UK Cambridge University Press 01.05.2004
Cambridge University Press (CUP)
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ISSN:0029-6651
1475-2719
DOI:10.1079/PNS2004358