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variable transposon epigenetic silencing underlies the variable mef2ca mutant bone phenotype, and could be a widespread mechanism of phenotypic variability in animals.
Mef2 (show MYEF2 Proteins) controls skeletal muscle formation after terminal differentiation.
Our study provides new insights in MEF2C conservation and provides the first evidence of mef2cb regulation by both transcriptional and post transcriptional mechanisms.
By selectively inhibiting translational initiation of mef2ca and other mRNAs, eIF4EBP3L reprograms the translational profile of muscle, enabling it to adjust to new environmental conditions.
find no evidence that the phenotypic stability in the wild type is provided by redundancy between mef2ca and its co-ortholog mef2cb, or that it is related to the selector (homeotic) gene function of mef2ca
Mef2ca single mutants have delayed heart development, but form an apparently normal heart. Mef2cb single mutants have a functional heart and are viable adults.
Data show that mef2cb is expressed in the late ventricular region, and is necessary for late myocardial addition to the arterial pole.
the genetic interaction of Tbx5 (show TBX5 Proteins) and Mef2c is not only required for MYH6 (show MYH6 Proteins) expression but also essential for the early stages of heart development and survival
Mef2c and Mef2d (show MEF2D Proteins) are required for proper cardiac gene expression.
a MEF2C and CEBPA correlation in CML disease progression
Single nucleotide polymorphism in MEF2C gene is associated with major depressive disorder.
we identified novel associations in WLS (show WLS Proteins) , ARHGAP1 (show ARHGAP1 Proteins) , and 5' of MEF2C ( P- values < 8x10 - 5 ; false discovery rate (FDR) q-values < 0.01) that were much more strongly associated with BMD (show BEST1 Proteins) compared to the GWAS SNPs.
Our analysis consistently identified significant sub-networks associated with the interacting transcription factors MEF2C and TWIST1 (show TWIST1 Proteins), genes not previously associated with spontaneous preterm births , both of which regulate processes clearly relevant to birth timing.
Key role for miR (show MLXIP Proteins)-214 in modulation of MEF2C-MYOCD-LMOD1 (show LMOD1 Proteins) signaling.
Endothelial Mef2c regulates the endothelial actin cytoskeleton and inhibits smooth muscle cell migration into the intima.
The mRNA expressions of PPP3CB (show PPP3CB Proteins) and MEF2C were significantly up-regulated, and CAMK1 (show CAMK1 Proteins) and PPP3R1 (show PPP3R1 Proteins) were significantly down-regulated in mitral regurgitation(MR) patients compared to normal subjects. Moreover, MR patients had significantly increased mRNA levels of PPP3CB (show PPP3CB Proteins), MEF2C and PLCE1 (show PLCE1 Proteins) compared to aortic valve disease patients
Findings suggest that a single introduction of the three cardiomyogenic transcription factor (GATA4 (show GATA4 Proteins), cand TBX5 (show TBX5 Proteins))genes using polyethyleneimine (PEI)-based transfection is sufficient for transdifferentiation of adipose-derived stem cells (hADSCs) towards the cardiomyogenic lineage.
Mef2c is highly expressed in the retina where it modulates photoreceptor-specific gene expression
Study provides evidence that Mef2c cooperated with Sp1 (show PSG1 Proteins) to activate human AQP1 (show AQP1 Proteins) transcription by binding to its proximal promoter in human umbilical cord vein endothelial cells indicating that AQP1 (show AQP1 Proteins) is a direct target of Mef2c in regulating angiogenesis and vasculogenesis of endothelial cells.
Deletion and mutation analyses of the promoter of pig myocyte enhancer factor 2 (MEF2 (show MYEF2 Proteins)) gene showed that MyoD (show MYOD1 Proteins) and MEF2 (show MYEF2 Proteins) binding sites within the Mef2c promoter were responsible for the regulation of Mef2c transcription. This study helped to clarify the regulation of Mef2c in muscle differentiation and regeneration.
The cDNA sequence was analyzed and the 5' upstream region of the mef2c gene was isolated from porcine genomic DNA.
analysis of sequence and variations of the bovine myocyte enhancer factor 2C (MEF2C) gene promoter in Bos taurus cattle
lf5 ChIP-seq revealed that Klf5 (show KLF5 Proteins) binding overlaps that of MyoD (show MYOD1 Proteins) and Mef2, and Klf5 (show KLF5 Proteins) physically associates with both MyoD (show MYOD1 Proteins) and Mef2. In addition, MyoD (show MYOD1 Proteins) recruitment was greatly reduced in the absence of Klf5 (show KLF5 Proteins). These results indicate that Klf5 (show KLF5 Proteins) is an essential regulator of skeletal muscle differentiation, acting in concert with myogenic transcription factors such as MyoD (show MYOD1 Proteins) and Mef2.
The authors show here that conditional embryonic deletion of Mef2c in cortical and hippocampal excitatory neurons (Emx1 (show EMX1 Proteins)-lineage) produces a dramatic reduction in cortical network activity in vivo, due in part to a dramatic increase in inhibitory and a decrease in excitatory synaptic transmission. Perturbing MEF2C function in neocortex can produce autistic- and intellectual disability-like behaviors in mice.
Here, the authors show that loss of Fxn (show FXN Proteins) in the nervous system in mice also activates an iron/sphingolipid/PDK1 (show PDPK1 Proteins)/Mef2 pathway, indicating that the mechanism is evolutionarily conserved.
Ca(2 (show CA2 Proteins)+) signaling pathway increases Nr4a1 (show NR4A1 Proteins) expression in MA-10 Leydig cells, at least in part, by enhancing the recruitment of coactivator most likely through the MEF2, AP1 (show JUN Proteins), and CREB (show CREB1 Proteins) transcription factors thus demonstrating an important interplay between the Ca(2 (show CA2 Proteins)+) and cAMP pathways in regulating Nr4a1 (show NR4A1 Proteins) expression.
HDAC5 (show HDAC5 Proteins) emerges as a cellular conductor of MEF2C and M6a (show GPM6A Proteins) activity and is regulated by miR (show MLXIP Proteins)-124 and miR (show MLXIP Proteins)-9 to control neurite development.
In cardiomyocytes exposed to biomechanical stimulation, FAK (show PTK2 Proteins) accumulates in the nucleus, binds to and upregulates the transcriptional activity of MEF2c through an interaction with the FAK (show PTK2 Proteins) focal adhesion targeting (FAT) domain.
In Fmr1 (show FMR1 Proteins) KO neurons, Mdm2 (show MDM2 Proteins) is hyperphosphorylated, nuclear localized basally, and unaffected by MEF2 activation, which our data suggest due to an enhanced interaction with Eukaryotic Elongation Factor (show TSFM Proteins) 1alpha (EF1alpha), whose protein levels are elevated in Fmr1 (show FMR1 Proteins) KO. Expression of a dephosphomimetic of Mdm2 (show MDM2 Proteins) rescues PSD-95 (show DLG4 Proteins) ubiquitination, degradation and synapse elimination in Fmr1 (show FMR1 Proteins) KO neurons.
two MEF2 sites in the enhancer function cooperatively due to bridging of the MEF2C-bound sites by the SAP domain-containing co-activator protein myocardin
Our results elucidate the specific role of the transcription factors CREB (show CREB1 Proteins), SRF, and MEF2 in the depression and potentiation components of ODP in vivo, therefore better informing future attempts to find therapeutic targets for diseases where activity-dependent plasticity is disrupted.
that Foxp2 (show FOXP2 Proteins)-Mef2C signaling is critical to corticostriatal circuit formation
This locus encodes a member of the MADS box transcription enhancer factor 2 (MEF2) family of proteins, which play a role in myogenesis. The encoded protein, MEF2 polypeptide C, has both trans-activating and DNA binding activities. This protein may play a role in maintaining the differentiated state of muscle cells. Mutations and deletions at this locus have been associated with severe mental retardation, stereotypic movements, epilepsy, and cerebral malformation. Alternatively spliced transcript variants have been described.
myocyte-specific enhancer factor 2C
, myocyte enhancer factor 2C
, myocyte-specific enhancer factor 2C-like
, MADS box transcription enhancer factor 2, polypeptide C
, MADS box transcription enhancer factor 2, polypeptide C (myocyte enhancer factor 2C)
, Myocyte enhancer factor 2C protein
, myocyte enhancer factor 2c