Follistatin-mediated skeletal muscle hypertrophy is regulated by Smad3 and mTOR independently of myostatin
Open accessAbstract
Follistatin is essential for skeletal muscle development and growth, but the intracellular signaling networks that regulate follistatin-mediated effects are not well defined. We show here that the administration of an adeno-associated viral vector expressing follistatin-288aa (rAAV6:Fst-288) markedly increased muscle mass and force-producing capacity concomitant with increased protein synthesis and mammalian target of rapamycin (mTOR) activation. These effects were attenuated by inhibition of mTOR or deletion of S6K1/2. Furthermore, we identify Smad3 as the critical intracellular link that mediates the effects of follistatin on mTOR signaling. Expression of constitutively active Smad3 not only markedly prevented skeletal muscle growth induced by follistatin but also potently suppressed follistatin-induced Akt/mTOR/S6K signaling. Importantly, the regulation of Smad3- and mTOR-dependent events by follistatin occurred independently of overexpression or knockout of myostatin, a key repressor of muscle development that can regulate Smad3 and mTOR signaling and that is itself inhibited by follistatin. These findings identify a critical role of Smad3/Akt/mTOR/S6K/S6RP signaling in follistatin-mediated muscle growth that operates independently of myostatin-driven mechanisms.
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Rapamycin treatment or mTOR knockdown reverts the hypertrophic effect of myostatin blockade, indicating cross-talk between myostatin and the AKT/mTOR axis.
“Indeed, rapamycin treatment or mTOR knockdown revert the hypertrophic effect of myostatin blockade17,18.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [18]
Inhibition of Smad2/3 is sufficient to promote muscle growth, suggesting that genes involved in protein turnover are targets of these transcription factors.
“Importantly, just inhibition of Smad2/3 is sufficient to promote muscle growth17,18, suggesting that genes involved in protein turnover are the target of these transcription factors.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [18]
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“, directly by mechanisms independent from MSTN [44,45].”
BackgroundMyokine/Adipokine response to “Aerobic” exercise: Is it just a matter of exercise load?
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“In turn, follistatin is a myostatin-binding protein that promotes skeletal muscle development through the activation of the mammalian target of rapamycin pathway (Winbanks et al., 2012).”
BackgroundDavey, J. R., Watt, K. I., Parker, B. L., Chaudhuri, R., Ryall, J. G., Cunningham, L., Qian, H., Sartorelli, V., Sandri, M., Chamberlain, J., et al. (2016) · JCI Insight · doi:10.1172/jci.insight.85477 · Cited by 51 · see citing works
Self-citation
- Authors
- Winbanks, C. E., Weeks, K. L., Thomson, R. E., Sepulveda, P. V., Beyer, C., Qian, H., Chen, J. L., Allen, J. M., Lancaster, G. I., Febbraio, M. A., Harrison, C. A., McMullen, J. R., Chamberlain, J. S., & Gregorevic, P.
- Affiliations
- Baker Heart and Diabetes Institute (AU)
- University of Washington (US)
- Prince Henry’s Institute of Medical Research, Victoria 3168, Australia 3
- Corresponding author
- Gregorevic, Paul
- ORCID
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2012-06-18
- Volume
- 197
- Issue
- 7
- Pages
- 997-1008
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC3384410
- OpenAlex
- W2154083884
- Cited by
- 218
- References
- 65
- Citations by year
- 2026: 10 · 2025: 15 · 2024: 21 · 2023: 13 · 2022: 21 · 2021: 18 · 2020: 15 · 2019: 13 · 2018: 9 · 2017: 21 · 2016: 15 · 2015: 17 · 2014: 10 · 2013: 15 · 2012: 4
- FWCI
- 5.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Minerva Access (University of Melbourne) (submittedVersion, cc-by-nc-sa)
- Funders
- National Institute on Aging (AG033610, R01AG033610)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Keywords
- follistatin, skeletal muscle hypertrophy, Smad3, mTOR signaling, myostatin, ribosomal protein S6, muscle mass, muscle force production, adeno-associated virus vectors, muscle growth regulation
- MeSH terms
- Animals, Humans, Hypertrophy, Mice, Inbred C57BL, Signal Transduction, Muscle, Skeletal, Follistatin, Mice, Smad3 Protein, Myostatin, HEK293 Cells, TOR Serine-Threonine Kinases
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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