Integrated expression analysis of muscle hypertrophy identifies Asb2 as a negative regulator of muscle mass
Open accessAbstract
The transforming growth factor-β (TGF-β) signaling network is a critical regulator of skeletal muscle mass and function and, thus, is an attractive therapeutic target for combating muscle disease, but the underlying mechanisms of action remain undetermined. We report that follistatin-based interventions (which modulate TGF-β network activity) can promote muscle hypertrophy that ameliorates aging-associated muscle wasting. However, the muscles of old sarcopenic mice demonstrate reduced response to follistatin compared with healthy young-adult musculature. Quantitative proteomic and transcriptomic analyses of young-adult muscles identified a transcription/translation signature elicited by follistatin exposure, which included repression of ankyrin repeat and SOCS box protein 2 ( Asb2 ). Increasing expression of ASB2 reduced muscle mass, thereby demonstrating that Asb2 is a TGF-β network–responsive negative regulator of muscle mass. In contrast to young-adult muscles, sarcopenic muscles do not exhibit reduced ASB2 abundance with follistatin exposure. Moreover, preventing repression of ASB2 in young-adult muscles diminished follistatin-induced muscle hypertrophy. These findings provide insight into the program of transcription and translation events governing follistatin-mediated adaptation of skeletal muscle attributes and identify Asb2 as a regulator of muscle mass implicated in the potential mechanistic dysfunction between follistatin-mediated muscle growth in young and old muscles.
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Follistatin-mediated hypertrophy not only blocks myostatin signaling but simultaneously stimulates Smad1/5/8 activation.
“Consistently, follistatin-mediated hypertrophy not only blocks myostatin signaling but simultaneously stimulates Smad1/5/8 activation19,22,23.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [22]
Asb2b is a muscle-specific ubiquitin ligase repressed by Follistatin and critical for hypertrophy; its inhibition is permissive for growth, while its overexpression causes muscle atrophy.
“An exception is the muscle-specific ubiquitin ligase, SOCS box protein 2 (Asb2b)22, which was identified to be repressed by Follistatin and to be critical for hypertrophy. In fact, while its inhibition is permissive for growth, its overexpression causes muscle atrophy22.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [22]
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- Authors
- Davey, J. R., Watt, K. I., Parker, B. L., Chaudhuri, R., Ryall, J. G., Cunningham, L., Qian, H., Sartorelli, V., Sandri, M., Chamberlain, J., James, D. E., & Gregorevic, P.
- Affiliations
- Baker Heart and Diabetes Institute (AU)
- The University of Sydney (AU)
- National Institutes of Health (US)
- University of Padua (IT)
- University of Washington (US)
- Corresponding author
- Gregorevic, Paul
- ORCID
- Venue
- JCI Insight
- Published
- 2016-04-21
- Volume
- 1
- Issue
- 5
- ISSN
- 2379-3708 (ISSN-L)
- PMC
- PMC4863241
- OpenAlex
- W2336035698
- Cited by
- 51
- References
- 55
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 9 · 2023: 2 · 2022: 2 · 2021: 11 · 2020: 5 · 2019: 7 · 2018: 4 · 2017: 4 · 2016: 1
- FWCI
- 2.77
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- JCI Insight (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Monash University Research Portal (Monash University) (submittedVersion, other-oa)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- University of Washington
- State Government of Victoria
- National Institutes of Health
- Medical Research Council
- National Health and Medical Research Council (1046782, 526648)
- National Institute on Aging (R01AG033610)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (U54AR065139, R01AR044533)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Health Sciences › Medicine › Physiology › Nutrition and Health in Aging
- Keywords
- ASB2, follistatin, muscle hypertrophy, skeletal muscle mass, TGF-beta signaling, sarcopenia, aging, muscle atrophy, transcriptional repression, translational regulation, proteomics, transcriptomics, negative regulator
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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