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An absolute requirement for either MyoD or Myf5 in muscle regeneration.
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MyoD signaling during myogenesis is regulated by HDAC1.
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Linc-RAM regulates expression of myogenic genes by directly binding MyoD, which in turn promotes the assembly of the MyoD-Baf60c-Brg1 complex on the regulatory elements of target genes.
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ACL regulates the net amount of acetyl groups available, leading to alterations in acetylation of H3(K9/14) and H3(K27) at the MYOD locus, thus increasing MYOD expression.
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Studies indicate MyoD displays function to regulate determination of skeletal muscle progenitors [Review].
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Muscle regulatory transcription factor MyoD regulates the expression of the pro-apoptotic Bcl2 family member PUMA by binding to the promoter region of PUMA. The increase in MyoD binding to the PUMA promoter as a consequence of culture in differentiation media (DM) is diminished in myoblasts silenced for MyoD expression. In myoblasts silenced for MyoD expression, p53 binding to the PUMA promoter is diminished in response
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our results indicate that HDAC11 would suppress myoblast differentiation via regulation of MyoD-dependent transcription. These findings suggest that HDAC11 is a novel critical target for controlling myoblast differentiation.
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The data showed that Mettl3 is required for MyoD mRNA expression in proliferative myoblasts.
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Gm7325, as a novel MyoD-target gene, is specifically induced in activated satellite cells, and may have an important role in skeletal myogenesis.
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The ELF-EMFs did not affect C2C12 myoblast viability or proliferation rate. Conversely, at ELF-EMF intensity in the mT range, the myogenic process was accelerated, through increased expression of MyoD, myogenin, and connexin 43
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In this study, we identified ubiquitin-specific protease 4 (USP4), one of deubiquitinating enzymes, as a suppressor of MRFs by demonstrating that a knockdown of USP4 enhances myogenesis by controlling MyoD and the level of myogenesis marker proteins in C2C12 cells... we propose that USP4 is a key player in myogenic differentiation; it controls myogenic regulatory factors in a catalytic-independent manner
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MyoD regulates the oxidative metabolic capacity of adult skeletal muscle;ChIP-seq analysis identified MyoD binding on the PGC-1b, but not PGC-1a, gene locus;MyoD cooperates with alternative NF-kappaB to regulate PGC-1b transcription; MyoD and RelB co-occupy many other genes involved in aerobic respiration
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LSD1 is required for the timely expression of MyoD in limb buds.
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bn1 expression is induced during myoblast differentiation, in a p38 MAP kinase- and MyoD- dependent manner. RNAi-mediated depletion of drebrin, or treatment with a chemical drebrin inhibitor, resulted in a similar phenotype in myoblasts: defective differentiation, with low levels of early and late differentiation markers and inefficient production of myofibers.
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Data show that MyoD and myogenin associate with distinct chromatin states.
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lf5 ChIP-seq revealed that Klf5 binding overlaps that of MyoD and Mef2, and Klf5 physically associates with both MyoD and Mef2. In addition, MyoD recruitment was greatly reduced in the absence of Klf5. These results indicate that Klf5 is an essential regulator of skeletal muscle differentiation, acting in concert with myogenic transcription factors such as MyoD and Mef2.
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Results indicate the importance of integrating histone modifications and MyoD chromatin binding for coordinated gene activation and repression during myogenic differentiation.
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Data suggest Tle3 plays role in regulation of MyoD1 function during myogenesis; up-regulation of Tle3 expression suppresses myogenesis; conversely, down-regulation of Tle3 expression promotes myogenesis/cell proliferation; Tle3 interferes with MyoD1 by disrupting association of basic helix-loop-helix domain of MyoD with E proteins. (Tle3 = transducin-like enhancer of split 3; MyoD1 = myogenic differentiation protein 1)
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significant co-localization of binding sites for MyoD and Six proteins on over a thousand mouse genomic DNA regions, were found.
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Through mutational analysis, we derive an optimally active phospho-mutant form of MyoD that has a dramatically enhanced ability to drive myogenic reprogramming in vivo. Mechanistically, this is achieved through increased protein stability and enhanced chromatin association. Therefore, multi-site phospho-regulation of class II bHLH proteins is conserved across cell lineages and germ layers, and manipulation of phosphorylat
