The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Histone modifications and exercise adaptations
Abstract
The spatial association between genomic DNA and histone proteins within chromatin plays a key role in the regulation of gene expression and is largely governed by post-translational modifications to histone proteins, particularly H3 and H4. These modifications include phosphorylation, acetylation, and mono-, di-, and tri-methylation, and while some are associated with transcriptional repression, acetylation of lysine residues within H3 generally correlates with transcriptional activation. Histone acetylation is regulated by the balance between the activities of histone acetyl transferase (HAT) and histone deacetylase (HDAC). In skeletal muscle, the class II HDACs 4, 5, 7, and 9 play a key role in muscle development and adaptation and have been implicated in exercise adaptations. As just one example, exercise results in the nuclear export of HDACs 4 and 5, secondary to their phosphorylation by CaMKII and AMPK, two kinases that are activated during exercise in response to changes in sarcoplasmic Ca(2+) levels and energy status, in association with increased GLUT4 expression in human skeletal muscle. Unraveling the complexities of the so-called "histone code" before and after exercise is likely to lead to a greater understanding of the regulation of exercise/activity-induced alterations in skeletal muscle gene expression and reinforce the importance of skeletal muscle plasticity in health and disease.
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“HDAC5 functions to acetylate histones, causing the chromatin to be wound tighter restricting the access of transcription factors to promoter regions [31].”
From New strategies in sport nutrition to increase exercise performance (2016) · cites this paper as [31]
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Cites
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
The Role of Chromatin during Transcription
Li, B., Carey, M., & Workman, J. L. (2007) · Cell · doi:10.1016/j.cell.2007.01.015 · Cited by 3,503
Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes
Wang, Z., Zang, C., Cui, K., Schones, D. E., Barski, A., Peng, W., & Zhao, K. (2009) · Cell · doi:10.1016/j.cell.2009.06.049 · Cited by 1,344
Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation
McKinsey, T. A., Zhang, C., Lu, J., & Olson, E. N. (2000) · Nature · doi:10.1038/35040593 · Cited by 1,051
Histone Deacetylase 4 Controls Chondrocyte Hypertrophy during Skeletogenesis
Vega, R. B., Matsuda, K., Oh, J., Barbosa, A. C. C., Yang, X., Meadows, E., McAnally, J., Pomajzl, C., Shelton, J. M., Richardson, J. A., et al. (2004) · Cell · doi:10.1016/j.cell.2004.10.024 · Cited by 805
Cotranscriptional Set2 Methylation of Histone H3 Lysine 36 Recruits a Repressive Rpd3 Complex
Keogh, M., Kurdistani, S. K., Morris, S. A., Ahn, S., Podolny, V., Collins, S. R., Schuldiner, M., Chin, K., Punna, T., Thompson, N. J., et al. (2005) · Cell · doi:10.1016/j.cell.2005.10.025 · Cited by 780
Fischle, W., Dequiedt, F., Hendzel, M. J., Guenther, M. G., Lazar, M. A., Voelter, W., & Verdin, E. (2002) · Molecular Cell · doi:10.1016/s1097-2765(01)00429-4 · Cited by 754
Chang, S., McKinsey, T. A., Zhang, C. L., Richardson, J. A., Hill, J. A., & Olson, E. N. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8467-8476.2004 · Cited by 612
Chromatin remodelling: the industrial revolution of DNA around histones
Saha, A., Wittmeyer, J., & Cairns, B. R. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1945 · Cited by 590
Lu, J., McKinsey, T. A., Zhang, C., & Olson, E. N. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00025-3 · Cited by 547
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Integrative Biology of Exercise
Hawley, J. A., Hargreaves, M., Joyner, M. J., & Zierath, J. R. (2014) · Cell · doi:10.1016/j.cell.2014.10.029 · Cited by 1,152
Self-citationDietary factors, epigenetic modifications and obesity outcomes: Progresses and perspectives
Milagro, F. I., Mansego, M. L., de Miguel, C., & Martínez, J. A. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.06.010 · Cited by 323
Egan, B., & Sharples, A. P. (2023) · Physiological Reviews · doi:10.1152/physrev.00054.2021 · Cited by 278
Nutrition, Epigenetics, and Metabolic Syndrome
Wang, J., Wu, Z., Li, D., Li, N., Dindot, S. V., Satterfield, M. C., Bazer, F. W., & Wu, G. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4381 · Cited by 266
New strategies in sport nutrition to increase exercise performance
Close, G. L., Hamilton, D. L., Philp, A., Burke, L. M., & Morton, J. P. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.01.016 · Cited by 221
Metadata
- Authors
- McGee, S. L., & Hargreaves, M.
- Affiliations
- Deakin University (AU)
- The University of Melbourne (AU)
- Corresponding author
- McGee, Sean L.
- Venue
- Journal of Applied Physiology
- Publisher
- American Physiological Society
- Published
- 2011-01
- Volume
- 110
- Issue
- 1
- Pages
- 258-263
- ISSN
- 0161-7567 (ISSN-L)
- 8750-7587
- 1522-1601
- OpenAlex
- W2152012558
- Cited by
- 120
- References
- 41
- Citations by year
- 2026: 7 · 2025: 5 · 2024: 5 · 2023: 8 · 2022: 8 · 2021: 4 · 2020: 4 · 2019: 14 · 2018: 9 · 2017: 9 · 2016: 7 · 2015: 8 · 2014: 10 · 2013: 9 · 2012: 5
- FWCI
- 0.62
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Applied Physiology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- histone modifications, exercise adaptation, skeletal muscle, histone acetylation, histone deacetylase, class II HDACs, histone acetyltransferase, histone methylation, histone phosphorylation, CaMKII, AMPK, GLUT4, nuclear export, histone code, gene expression regulation, muscle plasticity
- MeSH terms
- Adaptation, Physiological, Animals, Physical Exertion, Histones, Humans, Muscle Contraction, Muscle, Skeletal
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