Cited by 359Muscle Physiology and DisordersProtein Tyrosine PhosphatasesDevelopmental Biology and Gene Regulation

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Regulation of Distinct Stages of Skeletal Muscle Differentiation by Mitogen-Activated Protein Kinases

Bennett, Anton M., Tonks, Nicholas K.·1997·Science

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Abstract

The signal transduction pathway or pathways linking extracellular signals to myogenesis are poorly defined. Upon mitogen withdrawal from C2C12 myoblasts, the mitogen-activated protein kinase (MAPK) p42Erk2 is inactivated concomitant with up-regulation of muscle-specific genes. Overexpression of MAPK phosphatase-1 (MKP-1) inhibited p42Erk2 activity and was sufficient to relieve the inhibitory effects of mitogens on muscle-specific gene expression. Later during myogenesis, endogenous expression of MKP-1 decreased. MKP-1 overexpression during differentiation prevented myotube formation despite appropriate expression of myosin heavy chain. This indicates that muscle-specific gene expression is necessary but not sufficient to commit differentiated myocytes to myotubes and suggests a function for the MAPKs during the early and late stages of skeletal muscle differentiation.

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Role of the Ubiquitin-Proteasome Pathway in Regulating Abundance of the Cyclin-Dependent Kinase Inhibitor p27
Pagano, M., Tam, S. W., Theodoras, A. M., Beer‐Romero, P., Sal, G. D., Chau, V., Yew, P. R., Draetta, G. F., & Rolfe, M. (1995) · Science · doi:10.1126/science.7624798 · Cited by 1,815
Cyclin D1 Expression Is Regulated Positively by the p42/p44 and Negatively by the p38/HOG Pathway
Lavoie, J. N., L’Allemain, G., Brunet, A., Müller, R., & Pouysségur, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20608 · Cited by 1,210
MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo.
Sun, H., Charles, C. H., Lau, L. F., & Tonks, N. K. (1993) · Cell · doi:10.1016/0092-8674(93)90383-2 · Cited by 1,156
Correlation of Terminal Cell Cycle Arrest of Skeletal Muscle with Induction of p21 by MyoD
Halevy, O., Novitch, B. G., Spicer, D. B., Skapek, S. X., Rhee, J., Hannon, G. J., Beach, D., & Lassar, A. B. (1995) · Science · doi:10.1126/science.7863327 · Cited by 1,139
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 Regulation by Extracellular signals: Mechanisms and Specificity
Hill, C. S., & Treisman, R. (1995) · Cell · doi:10.1016/0092-8674(95)90403-4 · Cited by 1,012
Transforming p21 Mutants and c-Ets-2 Activate the Cyclin D1 Promoter through Distinguishable Regions
Albanese, C., Johnson, J., Watanabe, G., Eklund, N., Vu, D., Arnold, A., & Pestell, R. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.40.23589 · Cited by 802
bHLH factors in muscle development: dead lines and commitments, what to leave in and what to leave out.Preprint
Olson, E. N., & Klein, W. H. (1994) · Genes & Development · doi:10.1101/gad.8.1.1 · Cited by 684
MyoD-Induced Expression of p21 Inhibits Cyclin-Dependent Kinase Activity upon Myocyte Terminal Differentiation
Guo, K. Y., Wang, J., Andrés, V., Smith, R. C., & Walsh, K. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3823 · Cited by 422
Regulatory mechanisms that coordinate skeletal muscle differentiation and cell cycle withdrawal
Lassar, A. B., Skapek, S. X., & Novitch, B. G. (1994) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(94)90046-9 · Cited by 337

Show all 28 references

Research works printed but not linked: 7

Olson E. N., ibid. 4, 1454 (1990).
Dias P., Dilling M., Houghton P., Semin. Diagn. Pathol. 11, 3 (1994).
Vaidya T. B., Rhodes S. J., Taparowsky E. J., Konieczny S. F., Mol. Cell Biol. 9, 3576 (1989).
Cowley S., Paterson H., Kemp P., Marshall C. J., ibid. 77, 841 (1994);
Skapek S., Rhee J., Spicer D., Lassar A., ibid. 267, 1022 (1995).
Wang J., Walsh K., Cell Growth Differ. 7, 1471 (1996).
Rao S. S., Chu R. C., Kohtz D. S., Mol. Cell Biol. 14, 5259 (1994);

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Authors: Bennett, A. M., & Tonks, N. K.
Affiliations: Cold Spring Harbor Laboratory (US)
Corresponding author: Tonks, Nicholas K.
ORCID: Bennett, Anton M.
Tonks, Nicholas K.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1997-11-14
Volume: 278
Issue: 5341
Pages: 1288-1291
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.278.5341.1288
OpenAlex: W1975358464
Cited by: 359
References: 28
Citations by year: 2026: 2 · 2025: 4 · 2024: 8 · 2023: 5 · 2022: 4 · 2021: 14 · 2020: 10 · 2019: 5 · 2018: 12 · 2017: 9 · 2016: 9 · 2015: 7 · 2014: 13 · 2013: 12 · 2012: 11
FWCI: 7.23
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Keywords: skeletal muscle differentiation, myogenesis, mitogen-activated protein kinase, MAPK phosphatase-1, MKP-1, C2C12 myoblasts, muscle-specific gene expression, myotube formation, signal transduction, myosin heavy chain
MeSH terms: Animals, Cell Differentiation, Cell Division, Cell Line, Cloning, Molecular, Culture Media, Mitogens, Muscle Proteins, Phosphoprotein Phosphatases, Phosphorylation, Recombinant Fusion Proteins, Tetracycline, Transcription, Genetic, Signal Transduction, Protein Tyrosine Phosphatases, Calcium-Calmodulin-Dependent Protein Kinases, Immediate-Early Proteins, Muscle, Skeletal, Gene Expression Regulation, Developmental, Cell Cycle Proteins, Cyclin D1, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinases, JNK Mitogen-Activated Protein Kinases, Mice, Dual Specificity Phosphatase 1, Protein Phosphatase 1

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Regulation of Distinct Stages of Skeletal Muscle Differentiation by Mitogen-Activated Protein Kinases

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