BMP signaling controls muscle mass
Open accessAbstract
Cell size is determined by the balance between protein synthesis and degradation. This equilibrium is affected by hormones, nutrients, energy levels, mechanical stress and cytokines. Mutations that inactivate myostatin lead to excessive muscle growth in animals and humans, but the signals and pathways responsible for this hypertrophy remain largely unknown. Here we show that bone morphogenetic protein (BMP) signaling, acting through Smad1, Smad5 and Smad8 (Smad1/5/8), is the fundamental hypertrophic signal in mice. Inhibition of BMP signaling causes muscle atrophy, abolishes the hypertrophic phenotype of myostatin-deficient mice and strongly exacerbates the effects of denervation and fasting. BMP-Smad1/5/8 signaling negatively regulates a gene (Fbxo30) that encodes a ubiquitin ligase required for muscle loss, which we named muscle ubiquitin ligase of the SCF complex in atrophy-1 (MUSA1). Collectively, these data identify a critical role for the BMP pathway in adult muscle maintenance, growth and atrophy.
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BMP signaling converges on Smad4 and controls muscle mass.
“Another pathway that converges on Smad4 and controls muscle mass is BMP signaling19,20.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [19]
Inhibition of Atrogin-1 does not block denervation- and glucocorticoid-induced muscle loss and does not protect from aging sarcopenia.
“Inhibition of Atrogin-1 does not block denervation- and glucocorticoids-induced muscle loss19,44 and does not protect from aging sarcopenia46.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [19]
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 [19]
Specific ablation of Smad4 in the skeletal muscle of mice did not promote hypertrophy but caused atrophy and weakness.
“Interestingly, specific ablation of Smad4 in the skeletal muscle of mice did not promote hypertrophy but caused atrophy and weakness19.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [19]
Overexpression of the BMP antagonist noggin reverted the hypertrophic phenotype of myostatin knockout mice, arguing for genetic epistasis between the activin/myostatin and BMP pathways in muscle.
“The finding that overexpression of the BMP antagonist noggin reverted the hypertrophic phenotype of myostatin knockout mice, strongly argues in favor of genetic epistasis between the activin/myostatin and BMP pathways in muscle.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [19]
Inhibition of MUSA1 and SMART in denervated muscles via RNA-interference reduces the severity of neurogenic atrophy.
“Among these, inhibition of MUSA1 and SMART in denervated muscles via RNA-interference has been found to reduce the severity of neurogenic atrophy19,57.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [19]
Induction of BMP signaling activates Smad1/5/8, which with SMAD4 suppresses MUSA1 and activates mTOR-dependent protein synthesis.
“Induction of BMP signaling activates Smad1/5/8, which, together with SMAD 4, leads to the suppression of the MUSA1 [6] and the activation of mTOR-dependent protein synthesis [7].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [6]
BMP signaling is a positive regulator of muscle mass and is dominant over the myostatin pathway.
“On the other hand, BMP signaling is a positive regulator of muscle mass and is dominant over the myostatin pathway [6, 7].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [6]
BMP pathway is activated in myostatin knockout and is sufficient, when induced, to promote muscle growth and counteract muscle loss after denervation and in the absence of nutrients.
“BMP pathway is activated in myostatin knockout and is sufficient, when induced, to promote muscle growth and to counteract muscle loss after denervation and in the absence of nutrients [6–8].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [6]
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- Authors
- Sartori, R., Schirwis, E., Blaauw, B., Bortolanza, S., Zhao, J., Enzo, E., Stantzou, A., Mouisel, E., Toniolo, L., Ferry, A., Stricker, S., Goldberg, A. L., Dupont, S., Piccolo, S., Amthor, H., & Sandri, M.
- Affiliations
- University of Padua (IT)
- Centre National de la Recherche Scientifique (FR)
- Harvard University (US)
- Max Planck Institute for Molecular Genetics (DE)
- Hôpital Necker-Enfants Malades (FR)
- Corresponding author
- Piccolo, Stefano
- Amthor, Helge
- Sandri, Marco
- ORCID
- Venue
- Nature Genetics
- Published
- 2013-09-29
- Volume
- 45
- Issue
- 11
- Pages
- 1309-1318
- ISSN
- 1061-4036 (ISSN-L)
- 1546-1718
- OpenAlex
- W1997014674
- Cited by
- 467
- References
- 35
- Citations by year
- 2026: 29 · 2025: 26 · 2024: 25 · 2023: 31 · 2022: 43 · 2021: 37 · 2020: 38 · 2019: 42 · 2018: 37 · 2017: 33 · 2016: 45 · 2015: 41 · 2014: 35 · 2013: 4
- FWCI
- 18.65
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- Locations
- Nature Genetics (publishedVersion)
- PubMed (publishedVersion)
- MDC Repository (Max-Delbrueck-Center for Molecular Medicine) (submittedVersion)
- IRIS UNIMORE (University of Modena and Reggio Emilia) (submittedVersion, cc-by)
- Padua Research Archive (University of Padova) (submittedVersion)
- Zenodo (CERN European Organization for Nuclear Research) (submittedVersion, other-oa)
- 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 › Genetics › Neurogenetic and Muscular Disorders Research
- Keywords
- BMP signaling, muscle hypertrophy, muscle atrophy, myostatin, Smad1/5/8, ubiquitin ligase, denervation, fasting, muscle mass, protein synthesis and degradation
- MeSH terms
- Animals, Cell Line, Enzyme Activation, Humans, Mice, Inbred C57BL, Muscular Atrophy, Signal Transduction, Mice, Knockout, Muscle, Skeletal, Bone Morphogenetic Proteins, Gene Expression Profiling, RNA Interference, RNA, Small Interfering, Ubiquitin-Protein Ligases, Mice, Smad1 Protein, Smad4 Protein, Smad5 Protein, Smad8 Protein, Myostatin, HEK293 Cells
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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