Cited by 223Muscle Physiology and DisordersNutrition and Health in AgingMuscle metabolism and nutrition

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Stress-induced Skeletal Muscle Gadd45a Expression Reprograms Myonuclei and Causes Muscle Atrophy

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Ebert, Scott M., Dyle, Michael C., Kunkel, Steven D., Bullard, Steven A., Bongers, Kale S., Fox, Daniel K., Dierdorff, Jason M., Foster, Eric D., Adams, Christopher M.·2012·Journal of Biological Chemistry

DOI 10.1074/jbc.m112.374777PMC PMC3431665

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Abstract

Diverse stresses including starvation and muscle disuse cause skeletal muscle atrophy. However, the molecular mechanisms of muscle atrophy are complex and not well understood. Here, we demonstrate that growth arrest and DNA damage-inducible 45a protein (Gadd45a) is a critical mediator of muscle atrophy. We identified Gadd45a through an unbiased search for potential downstream mediators of the stress-inducible, pro-atrophy transcription factor ATF4. We show that Gadd45a is required for skeletal muscle atrophy induced by three distinct skeletal muscle stresses: fasting, muscle immobilization, and muscle denervation. Conversely, forced expression of Gadd45a in muscle or cultured myotubes induces atrophy in the absence of upstream stress. We show that muscle-specific ATF4 knock-out mice have a reduced capacity to induce Gadd45a mRNA in response to stress, and as a result, they undergo less atrophy in response to fasting or muscle immobilization. Interestingly, Gadd45a is a myonuclear protein that induces myonuclear remodeling and a comprehensive program for muscle atrophy. Gadd45a represses genes involved in anabolic signaling and energy production, and it induces pro-atrophy genes. As a result, Gadd45a reduces multiple barriers to muscle atrophy (including PGC-1α, Akt activity, and protein synthesis) and stimulates pro-atrophy mechanisms (including autophagy and caspase-mediated proteolysis). These results elucidate a critical stress-induced pathway that reprograms muscle gene expression to cause atrophy.

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RETRACTED: Increased muscle PGC-1α expression protects from sarcopenia and metabolic disease during aging
Wenz, T., Rossi, S. G., Rotundo, R. L., Spiegelman, B. M., & Moraes, C. T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911570106 · Cited by 600
Retracted
Applied Linear Regression Models
(1997) · Technometrics · doi:10.1080/00401706.1997.10485142 · Cited by 4,640
Identification of ubiquitin ligases required for skeletal muscle atrophy.
Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521
An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress
Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336
A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia
Kastan, M. B., Zhan, Q., El-Deiry, W. S., Carrier, F., Jacks, T., Walsh, W. V., Plunkett, B. S., Vogelstein, B., & Fornace, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90593-2 · Cited by 3,047
Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.
Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012
Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
Bodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752
The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors.
Stitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00211-4 · Cited by 1,964
FoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953
Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A., & Goldberg, A. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251541198 · Cited by 1,774

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He, F., Zhang, P., Liu, J., Wang, R., Kaufman, R. J., Yaden, B. C., & Karin, M. (2023) · Journal of Hepatology · doi:10.1016/j.jhep.2023.03.016 · Cited by 408
Hepatocyte-secreted DPP4 in obesity promotes adipose inflammation and insulin resistance
Ghorpade, D. S., Özcan, L., Zheng, Z., Nicoloro, S. M. C., Shen, Y., Chen, E., Blüher, M., Czech, M., & Tabas, I. A. (2018) · Nature · doi:10.1038/nature26138 · Cited by 295
Muscle Atrophy Induced by Mechanical Unloading: Mechanisms and Potential Countermeasures
Gao, Y., Arfat, Y., Wang, H., & Goswami, N. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00235 · Cited by 289
Mitophagy in tumorigenesis and metastasis
Poole, L. P., & Macleod, K. F. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03774-1 · Cited by 257
miR-29b contributes to multiple types of muscle atrophy
Li, J., Chan, M. C., Yu, Y., Bei, Y., Chen, P., Zhou, Q., Cheng, L., Chen, L., Ziegler, O., Rowe, G. C., et al. (2017) · Nature Communications · doi:10.1038/ncomms15201 · Cited by 246
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Fusakio, M. E., Willy, J. A., Wang, Y., Mirek, E. T., Al-Baghdadi, R. J. T., Adams, C. M., Anthony, T. G., & Wek, R. C. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-01-0039 · Cited by 238
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Emerging roles of ER stress and unfolded protein response pathways in skeletal muscle health and disease
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Authors: Ebert, S. M., Dyle, M. C., Kunkel, S. D., Bullard, S. A., Bongers, K. S., Fox, D. K., Dierdorff, J. M., Foster, E. D., & Adams, C. M.
Affiliations: University of Iowa (US)
Corresponding author: Adams, Christopher M.
ORCID: Ebert, Scott M.
Bongers, Kale S.
Adams, Christopher M.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2012-08
Volume: 287
Issue: 33
Pages: 27290-27301
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m112.374777
PMC: PMC3431665
OpenAlex: W2059083151
Cited by: 221
References: 63
Citations by year: 2026: 14 · 2025: 12 · 2024: 25 · 2023: 16 · 2022: 19 · 2021: 22 · 2020: 25 · 2019: 14 · 2018: 12 · 2017: 13 · 2016: 12 · 2015: 16 · 2014: 12 · 2013: 7 · 2012: 2
FWCI: 4.75
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 2991 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. Department of Veterans Affairs (I01 BX000976)
National Heart, Lung, and Blood Institute (HL-007121, T32HL007121)
National Institute of General Medical Sciences (T32 GM07361, T32GM007337)
National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR059115)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Health Sciences › Medicine › Physiology (medical) › Nutrition and Health in Aging
Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
Keywords: GADD45A, skeletal muscle atrophy, ATF4, muscle stress, fasting, muscle immobilization, muscle denervation, PGC-1α, Akt signaling, autophagy, protein synthesis, gene expression reprogramming
MeSH terms: Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, GADD45 Proteins, Animals, Cell Line, Cell Nucleus, Energy Metabolism, Gene Expression Regulation, Muscle Proteins, Muscular Atrophy, Nuclear Proteins, RNA, Messenger, Stress, Physiological, Transcription Factors, Protein Biosynthesis, Signal Transduction, Trans-Activators, Mice, Knockout, Muscle, Skeletal, Cell Cycle Proteins, Proto-Oncogene Proteins c-akt, Mice, Activating Transcription Factor 4

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Stress-induced Skeletal Muscle Gadd45a Expression Reprograms Myonuclei and Causes Muscle Atrophy

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