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Using a dominant-negative SmMef2 mutant, authors provide evidence that SmMef2 may regulate genes in the WNT (show WNT2 Proteins) pathway.
The authors identify and characterize Mef2 (show MYEF2 Proteins) from the schistosome worm Schistosoma mansoni (SmMef2).
in leiomyosarcomas (LMS), this two-faced trait of MEF2 is relevant for tumor aggressiveness. Class IIa HDACs are overexpressed in 22% of LMS, where high levels of MEF2, HDAC4 (show HDAC4 Proteins) and HDAC9 (show HDAC9 Proteins) inversely correlate with overall survival. The knock out of HDAC9 (show HDAC9 Proteins) suppresses the transformed phenotype of LMS cells, by restoring the transcriptional proficiency of some MEF2-target loci
The discovery of a novel MEF2A mutation in a Chinese family with premature CAD/MI suggests that MEF2A may have a significant role in the pathogenesis of premature CAD/MI.
The findings of this study are consistent with MEF2A deregulation conferring risk of formal thought disorder.
Variants in the 3'-UTR of MEF2A are associated with coronary artery disease in a Chinese Han population.
p38 MAPK (show MAPK14 Proteins) is a key regulator of canonical Wnt (show WNT2 Proteins) signaling by promoting a phospho-dependent interaction between MEF2 and beta-catenin (show CTNNB1 Proteins) to enhance cooperative transcriptional activity and cell proliferation.
Mechanistically, MEF-2 (show MYEF2 Proteins) was recruited to the viral promoter (LTR, long terminal repeat) in the context of chromatin, and constituted Tax (show CNTN2 Proteins)/CREB (show CREB1 Proteins) transcriptional complex via direct binding to the HTLV-1 LTR.
Our results revealed a link and interaction between MEF2A and miR (show MLXIP Proteins)-143 and suggested a potential mechanism for MEF2A to regulate H(2)O(2) -induced VSMC senescence.
six or seven amino acid deletions and synonymous mutations (147143G-->A)in exon 11 of the MEF2A gene may be correlated with susceptibility to coronary artery disease in the Chinese population
MEF2A is targeted to lysosomes for chaperone-mediated autophagy degradation; oxidative stress-induced (show SQSTM1 Proteins) lysosome destabilization leads to the disruption of MEF2A degradation as well as the dysregulation of its function
MEF2 transcription factors promotes epithelial-mesenchymal transition and invasiveness of hepatocellular carcinoma through TGF-beta1 (show TGFB1 Proteins) autoregulation circuitry.
Deficiency of AKT2 (show AKT2 Proteins) in myocardium results in diminished MEF2A abundance, which induced decreased size of cardiomyocytes. We additionally confirmed that EndoG (show ENDOG Proteins), which is also regulated by AKT2 (show AKT2 Proteins), is a suppressor of MEF2A in myocardium.
these data indicate that MEF2 (show MEF2C Proteins) and AP-1 (show JUN Proteins) confer antagonistic regulation of Hspb7 (show HSPB7 Proteins) gene expression in skeletal muscle, with implications for autophagy and muscle atrophy.
Nuclear HDAC4 (show HDAC5 Proteins) binds to chromatin as well as to MEF2A transcription factor, leading to histone deacetylation and altered neuronal gene expression. By using a Cdkl5 (show CDKL5 Proteins) knockout (Cdkl5 (show CDKL5 Proteins) -/Y) mouse model, we found that hypophosphorylated HDAC4 (show HDAC5 Proteins) translocates to the nucleus of neural precursor cells, thereby reducing histone 3 acetylation.
Knockdown of MEF2A significantly reduced hyperglycemia-induced cardiac fibroblast proliferation and migration, myofibroblast differentiation, matrix metalloproteinase activities, and collagen production.
Lentivirus-mediated MEF 2A shRNA accelerates inflammation and atherosclerosis in APOE (show APOE Proteins) knockout mice, but has no effect on lipoprotein levels in plasma.
microRNAs encoded by the Gtl2-Dio3 (show DIO3 Proteins) noncoding RNA locus function downstream of the MEF2A
Our results indicated that exercise-induced CPT1b (show CPT1B Proteins) expression was at least in part mediated by HDAC5 (show HDAC5 Proteins)/MEF2A interaction.
Whereas MEF2A is absolutely required for proper myoblast differentiation, MEF2B (show MEF2B Proteins), -C, and -D were found to be dispensable for this process.
A role for endogenous MEF2 (show MEF2C Proteins) factors exclusively in hormone/Fsk/cAMP-induced Nr4a1 (show NR4A1 Proteins) gene expression in mouse MA-10 Leydig cells.
These results show that NLK specifically regulates the MEF2A activity required for anterior formation in Xenopus development.
polymorphisms in the bovine MEF2A gene and their effect on the MEF2A mRNA expression level in the longissimus dorsi muscle
Mef2 (show MYEF2 Proteins) controls skeletal muscle formation after terminal differentiation.
Results suggest that myocyte-specific enhancer factor 2A is essential for cardiac contractility
Results suggest that myocyte enhancer factor 2A is essential for zebrafish posterior somite development.
The protein encoded by this gene is a DNA-binding transcription factor that activates many muscle-specific, growth factor-induced, and stress-induced genes. The encoded protein can act as a homodimer or as a heterodimer and is involved in several cellular processes, including muscle development, neuronal differentiation, cell growth control, and apoptosis. Defects in this gene could be a cause of autosomal dominant coronary artery disease 1 with myocardial infarction (ADCAD1). Several transcript variants encoding different isoforms have been found for this gene.
MADS box transcription enhancer factor 2, polypeptide A (myocyte enhancer factor 2A)
, myocyte-specific enhancer factor 2A
, serum response factor-like protein 1
, myocyte enhancer factor 2a
, myocyte-specific enhancer factor 2a
, myocyte-specific enhancer factor 2A homolog
, serum response factor-like protein 2
, myocyte enhancer factor 2A
, myocyte-specific enhancer factor 2A-like