Differentiation-dependent lysine 4 acetylation enhances MEF2C binding to DNA in skeletal muscle cells

Myocyte enhancer factor 2 (MEF2) proteins play a key role in promoting the expression of muscle-specific genes in differentiated muscle cells. MEF2 activity is regulated by the association with several transcriptional co-factors and by post-translational modifications. In the present report, we prov...

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Bibliographic Details
Published in:Nucleic acids research 2008-02, Vol.36 (3), p.915-928
Main Authors: Angelelli, Cecilia, Magli, Alessandro, Ferrari, Daniela, Ganassi, Massimo, Matafora, Vittoria, Parise, Flavia, Razzini, Giorgia, Bachi, Angela, Ferrari, Stefano, Molinari, Susanna
Format: Article
Language:English
Subjects:
Acetylation
Amino Acid Sequence
Animals
Binding Sites
Cell Differentiation
Cell Line
Chromatin - metabolism
DNA - metabolism
Electrophoretic Mobility Shift Assay
Fluorescence Recovery After Photobleaching
Lysine - metabolism
MEF2 Transcription Factors
Mice
Molecular Biology
Molecular Sequence Data
Muscle, Skeletal - cytology
Muscle, Skeletal - metabolism
Myogenic Regulatory Factors - chemistry
Myogenic Regulatory Factors - metabolism
Myogenin - genetics
p300-CBP Transcription Factors - metabolism
Protein Binding
Protein Processing, Post-Translational
Regulatory Elements, Transcriptional
Transcriptional Activation
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Summary:Myocyte enhancer factor 2 (MEF2) proteins play a key role in promoting the expression of muscle-specific genes in differentiated muscle cells. MEF2 activity is regulated by the association with several transcriptional co-factors and by post-translational modifications. In the present report, we provide evidence for a novel regulatory mechanism of MEF2C activity, which occurs at the onset of skeletal muscle differentiation and is based on Lys4 acetylation. This covalent modification results in the enhancement of MEF2C binding to DNA and chromatin. In particular, we report that the kinetic parameters of MEF2/DNA association change substantially upon induction of differentiation to give a more stable complex and that this effect is mediated by Lys4 acetylation. We also show that Lys4 acetylation plays a prominent role in the p300-dependent activation of MEF2C.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkm1114