scholarly journals Direct Interaction of Ca2+/Calmodulin Inhibits Histone Deacetylase 5 Repressor Core Binding to Myocyte Enhancer Factor 2

2003 ◽  
Vol 278 (20) ◽  
pp. 17625-17635 ◽  
Author(s):  
Imre Berger ◽  
Christoph Bieniossek ◽  
Christiane Schaffitzel ◽  
Markus Hassler ◽  
Eugenio Santelli ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Direct Interaction ◽  
Myocyte Enhancer Factor 2 ◽  
Myocyte Enhancer Factor ◽  
Enhancer Factor

scholarly journals Direct Interaction between Myocyte Enhancer Factor 2 (MEF2) and Protein Phosphatase 1α Represses MEF2-Dependent Gene Expression

2009 ◽  
Vol 29 (12) ◽  
pp. 3355-3366 ◽  
Author(s):  
R. L. S. Perry ◽  
C. Yang ◽  
N. Soora ◽  
J. Salma ◽  
M. Marback ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Protein Interactions ◽  
Protein Phosphatase ◽  
Hippocampal Neurons ◽  
Neuronal Cell ◽  
Direct Interaction ◽  
Myocyte Enhancer Factor 2 ◽  
Myocyte Enhancer Factor ◽  
Enhancer Factor

ABSTRACT The myocyte enhancer factor 2 (MEF2) transcription factors play important roles in neuronal, cardiac, and skeletal muscle tissues. MEF2 serves as a nuclear sensor, integrating signals from several signaling cascades through protein-protein interactions with kinases, chromatin remodeling factors, and other transcriptional regulators. Here, we report a novel interaction between the catalytic subunit of protein phosphatase 1α (PP1α) and MEF2. Interaction occurs within the nucleus, and binding of PP1α to MEF2 potently represses MEF2-dependent transcription. The interaction utilizes uncharacterized domains in both PP1α and MEF2, and PP1α phosphatase activity is not obligatory for MEF2 repression. Moreover, a MEF2-PP1α regulatory complex leads to nuclear retention and recruitment of histone deacetylase 4 to MEF2 transcription complexes. PP1α-mediated repression of MEF2 overrides the positive influence of calcineurin signaling, suggesting PP1α exerts a dominant level of control over MEF2 function. Indeed, PP1α-mediated repression of MEF2 function interferes with the prosurvival effect of MEF2 in primary hippocampal neurons. The PP1α-MEF2 interaction constitutes a potent locus of control for MEF2-dependent gene expression, having potentially important implications for neuronal cell survival, cardiac remodeling in disease, and terminal differentiation of vascular, cardiac, and skeletal muscle.

scholarly journals Histone Deacetylase 3 Interacts with and Deacetylates Myocyte Enhancer Factor 2

2006 ◽  
Vol 27 (4) ◽  
pp. 1280-1295 ◽  
Author(s):  
Serge Grégoire ◽  
Lin Xiao ◽  
Jianyun Nie ◽  
Xiaohong Zhang ◽  
Minghong Xu ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Thyroid Hormone Receptor ◽  
Trichostatin A ◽  
Hek293 Cells ◽  
Physical Interaction ◽  
Myocyte Enhancer Factor 2 ◽  
Specific Domain ◽  
Myocyte Enhancer Factor ◽  
Enhancer Factor

ABSTRACT The myocyte enhancer factor 2 (MEF2) family of transcription factors is not only important for controlling gene expression in normal cellular programs, like muscle differentiation, T-cell apoptosis, neuronal survival, and synaptic differentiation, but has also been linked to cardiac hypertrophy and other pathological conditions. Lysine acetylation has been shown to modulate MEF2 function, but it is not so clear which deacetylase(s) is involved. We report here that treatment of HEK293 cells with trichostatin A or nicotinamide upregulated MEF2D acetylation, suggesting that different deacetylases catalyze the deacetylation. Related to the trichostatin A sensitivity, histone deacetylase 4 (HDAC4) and HDAC5, two known partners of MEF2, exhibited little deacetylase activity towards MEF2D. In contrast, HDAC3 efficiently deacetylated MEF2D in vitro and in vivo. This was specific, since HDAC1, HDAC2, and HDAC8 failed to do so. While HDAC4, HDAC5, HDAC7, and HDAC9 are known to recognize primarily the MEF2-specific domain, we found that HDAC3 interacts directly with the MADS box. In addition, HDAC3 associated with the acetyltransferases p300 and p300/CBP-associated factor (PCAF) to reverse autoacetylation. Furthermore, the nuclear receptor corepressor SMRT (silencing mediator of retinoid acid and thyroid hormone receptor) stimulated the deacetylase activity of HDAC3 towards MEF2 and PCAF. Supporting the physical interaction and deacetylase activity, HDAC3 repressed MEF2-dependent transcription and inhibited myogenesis. These results reveal an unexpected role for HDAC3 and suggest a novel pathway through which MEF2 activity is controlled in vivo.

scholarly journals α-Actinin 4 Potentiates Myocyte Enhancer Factor-2 Transcription Activity by Antagonizing Histone Deacetylase 7

2006 ◽  
Vol 281 (46) ◽  
pp. 35070-35080 ◽  
Author(s):  
Sharmistha Chakraborty ◽  
Erin L. Reineke ◽  
Minh Lam ◽  
Xiaofang Li ◽  
Yu Liu ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Myocyte Enhancer Factor 2 ◽  
Transcription Activity ◽  
Myocyte Enhancer Factor ◽  
Enhancer Factor

scholarly journals AMP-activated Protein Kinase Regulates β-Catenin Transcription via Histone Deacetylase 5

2011 ◽  
Vol 286 (18) ◽  
pp. 16426-16434 ◽  
Author(s):  
Jun-Xing Zhao ◽  
Wan-Fu Yue ◽  
Mei-Jun Zhu ◽  
Min Du
Keyword(s):  
Cell Differentiation ◽  
Protein Kinase ◽  
Mrna Expression ◽  
Histone Deacetylase ◽  
Myocyte Enhancer Factor 2 ◽  
Myocyte Enhancer Factor ◽  
Ampk Activity ◽  
Underlying Mechanisms ◽  
Amp Activated Protein Kinase ◽  
Enhancer Factor

AMP-activated protein kinase (AMPK) is a key regulator of energy metabolism; it is inhibited under obese conditions and is activated by exercise and by many anti-diabetic drugs. Emerging evidence also suggests that AMPK regulates cell differentiation, but the underlying mechanisms are unclear. We hypothesized that AMPK regulates cell differentiation via altering β-catenin expression, which involves phosphorylation of class IIa histone deacetylase 5 (HDAC5). In both C3H10T1/2 cells and mouse embryonic fibroblasts (MEFs), AMPK activity was positively correlated with β-catenin content. Chemical inhibition of HDAC5 increased β-catenin mRNA expression. HDAC5 overexpression reduced and HDAC5 knockdown increased H3K9 acetylation and cellular β-catenin content. HDAC5 formed a complex with myocyte enhancer factor-2 to down-regulate β-catenin mRNA expression. AMPK phosphorylated HDAC5, which promoted HDAC5 exportation from the nucleus; mutation of two phosphorylation sites in HDAC5, Ser-259 and -498, abolished the regulatory role of AMPK on β-catenin expression. In conclusion, AMPK promotes β-catenin expression through phosphorylation of HDAC5, which reduces HDAC5 interaction with the β-catenin promoter via myocyte enhancer factor-2. Thus, the data indicate that AMPK regulates cell differentiation and development via cross-talk with the wingless and Int (Wnt)/β-catenin signaling pathway.

Regulation of hepatic stellate cell activation and growth by transcription factor myocyte enhancer factor 2

2004 ◽  
Vol 127 (4) ◽  
pp. 1174-1188 ◽  
Author(s):  
Xuemin Wang ◽  
Xiaoli Tang ◽  
Xiaoming Gong ◽  
Efsevia Albanis ◽  
Scott L. Friedman ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Hepatic Stellate Cell ◽  
Cell Activation ◽  
Stellate Cell ◽  
Myocyte Enhancer Factor 2 ◽  
Hepatic Stellate Cell Activation ◽  
Myocyte Enhancer Factor ◽  
Enhancer Factor
Sign in / Sign up

Export Citation Format

Share Document