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Related Concept Videos

Master Transcription Regulators02:23

Master Transcription Regulators

Master transcription regulators are regulatory proteins that are predominantly responsible for regulating the expression of multiple genes. Often these genes work in concert to drive a  complex process. Activation of a master transcription regulator can lead to a cascade of transcriptional activation necessary for that outcome. These regulators can directly bind to the regulatory sequences of the various genes involved, or they can indirectly regulate transcription by binding to regulatory...
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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Related Experiment Video

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Identification of MyoD Interactome Using Tandem Affinity Purification Coupled to Mass Spectrometry
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Published on: May 17, 2016

Exercise and MEF2-HDAC interactions.

Sean L McGee1

  • 1Department of Physiology, The University of Melbourne, Parkville, Victoria 3010, Australia.

Applied Physiology, Nutrition, and Metabolism = Physiologie Appliquee, Nutrition Et Metabolisme
|December 7, 2007
PubMed
Summary
This summary is machine-generated.

Exercise boosts skeletal muscle

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Last Updated: Jul 9, 2026

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Simultaneous Measurement of HDAC1 and HDAC6 Activity in HeLa Cells Using UHPLC-MS
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Published on: August 10, 2017

Area of Science:

  • Molecular Biology
  • Exercise Physiology
  • Skeletal Muscle Metabolism

Background:

  • Exercise enhances skeletal muscle metabolic capacity, improving energy balance and overall health.
  • This adaptation involves increased expression of metabolic enzymes, primarily regulated at the transcriptional level.
  • Class II histone deacetylases (HDACs), like HDAC5, act as transcriptional repressors, influencing these genes.

Purpose of the Study:

  • To investigate the molecular mechanisms by which exercise influences skeletal muscle gene expression.
  • To explore the role of HDAC5 and its interacting kinases in exercise-induced transcriptional regulation.
  • To understand how these pathways contribute to skeletal muscle adaptation to physical activity.

Main Methods:

  • Analysis of gene expression in skeletal muscle.
  • Investigating the interaction between HDAC5 and myocyte enhancer factor 2 (MEF2) transcription factors.
  • Studying the activity of HDAC5 kinases, such as 5'-AMP-activated protein kinase (AMPK) and protein kinase D (PKD).

Main Results:

  • Exercise increases the expression of metabolic enzymes in skeletal muscle.
  • HDAC5 interacts with MEF2 transcription factors to regulate gene expression.
  • HDAC5 kinases (AMPK, PKD) inactivate HDAC5 and promote its nuclear export, affecting gene transcription.

Conclusions:

  • Exercise-induced gene expression in skeletal muscle is mediated by the regulation of HDAC5 activity.
  • Kinase-dependent inactivation and nuclear export of HDAC5 are key mechanisms for exercise adaptation.
  • These molecular pathways are crucial for skeletal muscle's response to exercise.