Cited by 402TGF-β signaling in diseasesMuscle Physiology and DisordersDevelopmental Biology and Gene Regulation

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TGF-β inhibits muscle differentiation through functional repression of myogenic transcription factors by Smad3

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Liu, Dong, Black, Brian L., Derynck, Rik·2001·Genes & Development

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Abstract

Transforming growth factor-β (TGF-β) is a potent inhibitor of skeletal muscle differentiation, but the molecular mechanism and signaling events that lead to this inhibition are poorly characterized. Here we show that the TGF-β intracellular effector Smad3, but not Smad2, mediates the inhibition of myogenic differentiation in MyoD-expressing C3H10T1/2 cells and C2C12 myoblasts by repressing the activity of the MyoD family of transcriptional factors. The Smad3-mediated repression was directed at the E-box sequence motif within muscle gene enhancers and the bHLH region of MyoD, the domain required for its association with E-protein partners such as E12 and E47. The repression could be overcome by supplying an excess of E12, and covalent tethering of E47 to MyoD rendered the E-box-dependent transcriptional activity refractory to the effects of Smad3 and TGF-β. Smad3 physically interacted with the HLH domain of MyoD, and this interaction correlated with the ability of Smad3 to interfere with MyoD/E protein heterodimerization and binding of MyoD complexes to oligomerized E-box sites. Together, these results reveal a model for how TGF-β, through Smad3-mediated transcriptional repression, inhibits myogenic differentiation.

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Expression of a single transfected cDNA converts fibroblasts to myoblasts
Davis, R. L., Weintraub, H. M., & Lassar, A. B. (1987) · Cell · doi:10.1016/0092-8674(87)90585-x · Cited by 3,388
A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins
Murre, C., Page-McCaw, P., & Baltimore, D. (1989) · Cell · doi:10.1016/0092-8674(89)90682-x · Cited by 2,713
The protein Id: A negative regulator of helix-loop-helix DNA binding proteins
Benezra, R., Davis, R. L., Lockshon, D., Turner, D. L., & Weintraub, H. M. (1990) · Cell · doi:10.1016/0092-8674(90)90214-y · Cited by 2,202
Transcriptional control by the TGF‐β/Smad signaling system
Massagué, J., & Wotton, D. (2000) · The EMBO Journal · doi:10.1093/emboj/19.8.1745 · Cited by 1,990
The MyoD family and myogenesis: Redundancy, networks, and thresholds
Weintraub, H. (1993) · Cell · doi:10.1016/0092-8674(93)90610-3 · Cited by 1,057
TRANSCRIPTIONAL CONTROL OF MUSCLE DEVELOPMENT BY MYOCYTE ENHANCER FACTOR-2 (MEF2) PROTEINS
Black, B. L., & Olson, E. N. (1998) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.14.1.167 · Cited by 1,037
Self-citation
Transcriptional Activators of TGF-β Responses: Smads
Derynck, R., Zhang, Y. E., & Feng, X. (1998) · Cell · doi:10.1016/s0092-8674(00)81696-7 · Cited by 1,030
Self-citation
A novel human muscle factor related to but distinct from MyoD1 induces myogenic conversion in 10T1/2 fibroblasts.
Braun, T. W., Buschhausen-Denker, G., Bober, E., Tannich, E., & Arnold, H.-H. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03429.x · Cited by 906
Receptor-associated Mad homologues synergize as effectors of the TGF-β response
Zhang, Y. E., Feng, X., Wu, R.-Y., & Derynck, R. (1996) · Nature · doi:10.1038/383168a0 · Cited by 873
Self-citation
Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo
Lassar, A. B., Davis, R. L., Wright, W. E., Kadesch, T. R., Murre, C., Voronova, A., Baltimore, D., & Weintraub, H. M. (1991) · Cell · doi:10.1016/0092-8674(91)90620-e · Cited by 836

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Reviewer #1 (Public Review): Human myogenic progenitor cells display tenogenic differentiation potential and facilitate tendon regeneration
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Reviewer #2 (Public Review): Human myogenic progenitor cells display tenogenic differentiation potential and facilitate tendon regeneration
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Additional file 5 of Skeletal muscle regeneration failure in ischemic-damaged limbs is associated with pro-inflammatory macrophages and premature differentiation of satellite cells
Southerland, K. W., Xu, Y., Peters, D. T., Lin, X., Wei, X., Xiang, Y., Fei, K., Olivere, L. A., Morowitz, J. M., Otto, J. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26638317
Additional file 1 of Skeletal muscle regeneration failure in ischemic-damaged limbs is associated with pro-inflammatory macrophages and premature differentiation of satellite cells
Southerland, K. W., Xu, Y., Peters, D., Lin, X., Wei, X., Xiang, Y., Fei, K., Olivere, L. A., Morowitz, J. M., Otto, J. C., et al. (2023) · Figshare · doi:10.6084/m9.figshare.24546901
Additional file 3 of Skeletal muscle regeneration failure in ischemic-damaged limbs is associated with pro-inflammatory macrophages and premature differentiation of satellite cells
Southerland, K. W., Xu, Y., Peters, D. T., Lin, X., Wei, X., Xiang, Y., Fei, K., Olivere, L. A., Morowitz, J. M., Otto, J. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26638311
Additional file 2 of Skeletal muscle regeneration failure in ischemic-damaged limbs is associated with pro-inflammatory macrophages and premature differentiation of satellite cells
Southerland, K. W., Xu, Y., Peters, D., Lin, X., Wei, X., Xiang, Y., Fei, K., Olivere, L. A., Morowitz, J. M., Otto, J. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.24547047
Additional file 4 of Skeletal muscle regeneration failure in ischemic-damaged limbs is associated with pro-inflammatory macrophages and premature differentiation of satellite cells
Southerland, K. W., Xu, Y., Peters, D. T., Lin, X., Wei, X., Xiang, Y., Fei, K., Olivere, L. A., Morowitz, J. M., Otto, J. C., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26638314
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Authors: Liu, D., Black, B. L., & Derynck, R.
Affiliations: University of California, San Francisco (US)
ORCID: Liu, Dong
Black, Brian L.
Derynck, Rik
Venue: Genes & Development
Publisher: Cold Spring Harbor Laboratory
Published: 2001-11-15
Volume: 15
Issue: 22
Pages: 2950-2966
ISSN: 0890-9369 (ISSN-L)
1549-5477
DOI: 10.1101/gad.925901
PMC: PMC312830
OpenAlex: W2116961946
Cited by: 399
References: 80
Citations by year: 2026: 9 · 2025: 12 · 2024: 22 · 2023: 16 · 2022: 23 · 2021: 16 · 2020: 11 · 2019: 26 · 2018: 19 · 2017: 13 · 2016: 19 · 2015: 13 · 2014: 9 · 2013: 27 · 2012: 14
Type: posted content
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Genes & Development (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Cancer Institute (R01CA063101, R01-CA63101)
National Institute of Dental and Craniofacial Research (P60DE013058, P60 DE-13058)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Keywords: TGF-beta, Smad3, Smad2, skeletal muscle differentiation, myogenesis, MyoD, E-box, bHLH transcription factors, E12, E47, E protein, transcriptional repression, heterodimerization, C2C12 myoblasts, C3H10T1/2 cells
MeSH terms: Animals, Cell Differentiation, Cell Line, Cells, Cultured, DNA-Binding Proteins, Glutathione Transferase, Luciferases, Microscopy, Fluorescence, Plasmids, Protein Binding, Recombinant Fusion Proteins, Retroviridae, Transcription, Genetic, Transfection, Blotting, Western, Signal Transduction, Trans-Activators, Transforming Growth Factor beta, Protein Structure, Tertiary, MyoD Protein, Muscle, Skeletal, Dimerization, COS Cells, Mice, Smad3 Protein

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TGF-β inhibits muscle differentiation through functional repression of myogenic transcription factors by Smad3

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