Cited by 120Genomics and Chromatin DynamicsHistone Deacetylase Inhibitors ResearchMuscle Physiology and Disorders

Histone modifications and exercise adaptations

McGee, Sean L., Hargreaves, Mark·2011·Journal of Applied Physiology

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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Crossref · 10.1152/japplphysiol.00979.2010

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41 of 41 references verified0 citation errors · 0 not checkable

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  • HDAC5 functions to acetylate histones, causing chromatin to be wound tighter and restricting the access of transcription factors to promoter regions.

    “HDAC5 functions to acetylate histones, causing the chromatin to be wound tighter restricting the access of transcription factors to promoter regions [31].”

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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
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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