Identification of ubiquitin ligases required for skeletal muscle atrophy.
Open accessAbstract
Skeletal muscle adapts to decreases in activity and load by undergoing atrophy. To identify candidate molecular mediators of muscle atrophy, we performed transcript profiling. Although many genes were up-regulated in a single rat model of atrophy, only a small subset was universal in all atrophy models. Two of these genes encode ubiquitin ligases: Muscle RING Finger 1 ( MuRF1 ), and a gene we designate Muscle Atrophy F-box ( MAFbx ), the latter being a member of the SCF family of E3 ubiquitin ligases. Overexpression of MAFbx in myotubes produced atrophy, whereas mice deficient in either MAFbx or MuRF1 were found to be resistant to atrophy. These proteins are potential drug targets for the treatment of muscle atrophy.
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MuRF1 and Atrogin-1 are key factors for ubiquitin-proteasome system-mediated protein degradation in muscle atrophy.
“The E3 ligase muscle RING‐finger protein‐1 (MuRF1), encoded by Trim63, and the F‐Box protein Atrogin‐1, encoded by Fbxo32, are key factors for ubiquitin‐proteasome system‐mediated protein degradation in muscle atrophy.”
From Sepsis induces interleukin 6, gp130/JAK2/STAT3, and muscle wasting (2022) · cites this paper as [7]
The main text (page unavailable) calls MuRF1 and MAFbx critical regulators of muscle atrophy and describes their role as ubiquitin ligases that target proteins for proteasomal degradation. It qualifies their regulation of muscle-protein degradation as “most likely,” rather than establishing that mechanism definitively. The copy uses MAFbx and does not verify the Atrogin-1, Trim63, or Fbxo32 names in the citing sentence. (LLM, conf=0.83)
Experimental — accuracy not yet measuredA study examining MuRF1 and Atrogin1 gene expression in several models of muscle atrophy has reported that their gene expression is up-regulated at different time points.
“A study examining MuRF1 and Atrogin1 gene expression in several models of muscle atrophy has also reported that their gene expression is up-regulated at different time points (Bodine et al., 2001).”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Bodine et al., 2001
MuRF1 knockout mice are not protected from denervation-induced muscle loss at 7 days and only partially protected (around 30%) at 14 days; absence of MuRF1 does not protect from fasting or microgravity-induced atrophy, while muscle mass is spared following glucocorticoid treatment.
“MuRF1 knockout mice are not protected from denervation-induced muscle loss at 7 days and only partially protected (around 30%) at 14 days39. Moreover, the absence of MuRF1 does not protect from fasting or microgravity induced atrophy, while muscle mass is spared following glucocorticoid treatment43,44.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [39]
Atrogin-1/MAFbx and MuRF1 are the first ubiquitin ligases identified to play a role in muscle loss, are strongly upregulated in all catabolic conditions so far tested in animals, and are considered the master genes of muscle atrophy.
“The first ubiquitin ligases that were identified to play a role in muscle loss were Atrogin-1/MAFbx and MuRF1. These two E3s are strongly upregulated in all the catabolic conditions so far tested in animals and are considered the master genes of muscle atrophy39.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [39]
Genes encoding glycolysis and oxidative phosphorylation enzymes are coordinately suppressed in atrophying muscles during denervation, disuse, diabetes, cancer, fasting, and chronic kidney disease.
“Genes encoding for glycolysis and oxidative phosphorylation enzymes are coordinately suppressed in atrophying muscles during denervation, disuse, diabetes, cancer, fasting, and chronic kidney disease [10, 11, 13, 20].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [10]
Muscle atrophy requires activation of gene transcription programs that regulate expression of atrophy-related genes (atrogenes).
“Muscle atrophy requires the activation of gene transcription programs that regulate the expression of a subset of genes that are named atrophy-related genes or atrogenes [10–14].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [10]
Animal models that lack MURF-1 expression are protected from atrophy.
“Animal models that lack MURF-1 expression are protected from atrophy [71,72].”
From Omega-3 Fatty Acids and Skeletal Muscle Health (2015) · cites this paper as [71]
Mice deficient in either MAFbx or MuRF1 are resistant to atrophy.
“Mice deficient in either MAFbx or MuRF1 were demonstrated to be resistant to atrophy [7].”
From Nutraceuticals in the Prevention and Treatment of the Muscle Atrophy (2021) · cites this paper as [7]
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“Their role in muscle-mass regulation is supported by the finding that muscle atrophy induced by denervation is partially prevented in both MuRF1 null and atrogin1/MAFbx null mice [ 92 ].”
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- Authors
- Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., Pan, Z.-Q., Valenzuela, D. M., DeChiara, T. M., Stitt, T. N., Yancopoulos, G. D., & Glass, D. J.
- Affiliations
- Regeneron (United States) (US)
- Applied Biosystems, 850 Lincoln Center Drive, Foster City, CA 94404, USA.
- Regeneron Pharmaceuticals, 777 Old Saw Mill River Road, Tarrytown, NY, 10591–6707, USA.
- Icahn School of Medicine at Mount Sinai (US)
- Corresponding author
- Glass, David J.
- ORCID
- Venue
- Science
- Published
- 2001-11-23
- Volume
- 294
- Issue
- 5547
- Pages
- 1704-1708
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2167033587
- Cited by
- 3,521
- References
- 18
- Citations by year
- 2026: 124 · 2025: 133 · 2024: 141 · 2023: 139 · 2022: 157 · 2021: 151 · 2020: 202 · 2019: 175 · 2018: 180 · 2017: 175 · 2016: 175 · 2015: 178 · 2014: 182 · 2013: 190 · 2012: 173
- FWCI
- 15.71
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Keywords
- skeletal muscle atrophy, ubiquitin ligase, MuRF1, atrogin-1, SCF ubiquitin ligase, F-box protein, myotubes
- MeSH terms
- Amino Acid Sequence, Animals, Cloning, Molecular, Creatine Kinase, DNA-Binding Proteins, Humans, Immobilization, Isoenzymes, Molecular Sequence Data, Muscle Denervation, Muscle Proteins, Muscular Atrophy, Peptide Synthases, Phenotype, Protein Binding, RNA, Messenger, Trans-Activators, Up-Regulation, Rats, Sprague-Dawley, Gene Deletion, MyoD Protein, Myogenin, Mice, Knockout, Muscle, Skeletal, Hindlimb Suspension, Gene Expression Profiling, SKP Cullin F-Box Protein Ligases, Mice, Rats, Myogenic Regulatory Factor 5, Creatine Kinase, MM Form
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