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What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
Abstract
Studies of many different rodent models of muscle wasting have indicated that accelerated proteolysis via the ubiquitin-proteasome pathway is the principal cause of muscle atrophy induced by fasting, cancer cachexia, metabolic acidosis, denervation, disuse, diabetes, sepsis, burns, hyperthyroidism and excess glucocorticoids. However, our understanding about how muscle proteins are degraded, and how the ubiquitin-proteasome pathway is activated in muscle under these conditions, is still very limited. The identities of the important ubiquitin-protein ligases in skeletal muscle, and the ways in which they recognize substrates are still largely unknown. Recent in-vitro studies have suggested that one set of ubquitination enzymes, E2(14K) and E3(alpha), which are responsible for the 'N-end rule' system of ubiquitination, plays an important role in muscle, especially in catabolic states. However, their functional significance in degrading different muscle proteins is still unclear. This review focuses on the many gaps in our understanding of the functioning of the ubiquitin-proteasome pathway in muscle atrophy, and highlights the strengths and limitations of the different experimental approaches used in such studies.
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“These two systems are controlled by a transcriptional program that upregulates several crucial and rate-limiting enzymes (Glass, 2010; Jagoe and Goldberg, 2001).”
From Proteasome dysfunction induces muscle growth defects and protein aggregation (2014) · cites this paper as Jagoe and Goldberg, 2001
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Metadata
- Authors
- Jagoe, R. T., & Goldberg, A. L.
- Affiliations
- Harvard University (US)
- Corresponding author
- Goldberg, Alfred L.
- Venue
- Current Opinion in Clinical Nutrition and Metabolic Care
- Published
- 2001-05
- Volume
- 4
- Issue
- 3
- Pages
- 183-190
- ISSN
- 1363-1950 (ISSN-L)
- OpenAlex
- W2024946243
- Cited by
- 399
- References
- 1
- Citations by year
- 2025: 6 · 2024: 5 · 2023: 7 · 2022: 10 · 2021: 9 · 2020: 6 · 2019: 13 · 2018: 9 · 2017: 6 · 2016: 20 · 2015: 16 · 2014: 18 · 2013: 19 · 2012: 26
- FWCI
- 1.43
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Clinical Nutrition & Metabolic Care (publishedVersion)
- PubMed (publishedVersion)
- Funders
- ALS Association
- Muscular Dystrophy Association
- US-UK Fulbright Commission
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- ubiquitin-proteasome system, muscle atrophy, skeletal muscle protein degradation, ubiquitin-protein ligase, N-end rule, E2 ubiquitin-conjugating enzyme, E3 ubiquitin ligase, cachexia, denervation, disuse, glucocorticoids, metabolic acidosis, sepsis, burns, hyperthyroidism, diabetes mellitus
- MeSH terms
- Animals, Cysteine Endopeptidases, Humans, Multienzyme Complexes, Muscle Proteins, Muscular Atrophy, RNA, Messenger, Ubiquitins, Cysteine Proteinase Inhibitors, Muscle, Skeletal, Wasting Syndrome, Culture Techniques, Proteasome Endopeptidase Complex
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