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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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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