Ubiquitin-proteasome-dependent proteolysis in skeletal muscle.

Attaix, Didier; Aurousseau, Eveline; Combaret, Lydie; Kee, Anthony; Larbaud, Daniel; Rallière, Cécile; Souweine, Bertrand; Taillandier, Daniel; Tilignac, Thomas

doi:10.1051/rnd:19980202

Cited by 109Ubiquitin and proteasome pathwaysMuscle Physiology and DisordersMuscle metabolism and nutrition

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Ubiquitin-proteasome-dependent proteolysis in skeletal muscle.

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Attaix, Didier, Aurousseau, Eveline, Combaret, Lydie, Kee, Anthony, Larbaud, Daniel, Rallière, Cécile, Souweine, Bertrand, Taillandier, Daniel, Tilignac, Thomas·1998·Reproduction Nutrition Development

DOI 10.1051/rnd:19980202

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Abstract

The ubiquitin-proteasome proteolytic pathway has recently been reported to be of major importance in the breakdown of skeletal muscle proteins.The first step in this pathway is the cova- lent attachment of polyubiquitin chains to the targeted protein.Polyubiquitylated proteins are then recognized and degraded by the 26S proteasome complex.In this review, we critically analyse recent findings in the regulation of this pathway, both in animal models of muscle wasting and in some human diseases.The identification of regulatory steps of ubiquitin conjugation to protein substrates and/or of the proteolytic activities of the proteasome should lead to new concepts that can be used to manipulate muscle protein mass.Such concepts are essential for the devel- opment of anti-cachectic therapies for many clinical situations.@ Inra/Elsevier, Paris skeletal muscle / protein breakdown / ubiquitin / proteasome Résumé -Protéolyse musculaire ubiquitine-protéasome dépendante.Il a été récemmment démontré que la protéolyse ubiquitine-protéasome dépendante joue un rôle majeur dans la dégradation des protéines musculaires.La première étape de cette voie protéolytique correspond à la fixation covalente de chaînes polyubiquitylées sur les substrats protéiques.Ces protéines polyubiquitylées sont ultérieurement spécifiquement reconnues et dégradées par le protéasome 26S.Les derniers progrès accomplis dans la compréhension de la régulation de ce système dans les modèles animaux de fontes protéiques musculaires, et dans certaines situations cliniques, sont ana- lysés de façon critique dans cette revue bibliographique.L'identification d'étapes régulatrices de 1'ubiquitylation des substrats protéiques, et/ou des activités protéolytiques du protéasome, devrait conduire à de nouveaux concepts utilisables pour manipuler le dépôt des protéines musculaires.En particulier, ces concepts sont indispensables au développement de traitements anti-cachectiques dans de nombreuses situations cliniques.

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In muscle, proteolysis by the UPS is a major mechanism involved in myofibrillar protein degradation.
“Especially in muscle, proteolysis by the UPS is a major mechanism involved in myofibrillar protein degradation (Attaix et al., 1998; Hasselgren et al., 2002).”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Attaix et al., 1998

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Mechanisms of ubiquitination and proteasome-dependent proteolysis in skeletal muscle.
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The ubiquitin-dependent proteolytic pathway in skeletal muscle: its role in pathological states
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Authors: Attaix, D., Aurousseau, E., Combaret, L., Kee, A., Larbaud, D., Rallière, C., Souweine, B., Taillandier, D., & Tilignac, T.
Affiliations: Centre de Recherche en Nutrition Humaine d'Auvergne (FR)
ORCID: Attaix, Didier
Combaret, Lydie
Kee, Anthony
Souweine, Bertrand
Taillandier, Daniel
Venue: Reproduction Nutrition Development
Publisher: EDP Sciences
Published: 1998
Volume: 38
Issue: 2
Pages: 153-165
ISSN: 0003-388X (ISSN-L)
0926-5287
DOI: 10.1051/rnd:19980202
OpenAlex: W2102589258
Cited by: 109
References: 50
Citations by year: 2025: 1 · 2022: 4 · 2021: 1 · 2020: 4 · 2019: 1 · 2018: 3 · 2017: 2 · 2015: 1 · 2014: 2 · 2013: 4 · 2012: 3
FWCI: 0.65
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: annales de biologie animale biochimie biophysique (publishedVersion)
PubMed (publishedVersion)
Springer Link (Chiba Institute of Technology) (submittedVersion)
HAL (submittedVersion, other-oa)
HAL (submittedVersion)
Funders: Institut National de la Recherche Agronomique
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
Keywords: ubiquitin-proteasome system, skeletal muscle protein degradation, polyubiquitination, 26S proteasome, muscle atrophy, cachexia
MeSH terms: Animals, Cysteine Endopeptidases, Humans, Multienzyme Complexes, Muscle Proteins, Endopeptidases, Ubiquitins, Muscle, Skeletal, Proteasome Endopeptidase Complex

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Ubiquitin-proteasome-dependent proteolysis in skeletal muscle.

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