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Gene Review

MYOD1  -  myogenic differentiation 1

Gallus gallus

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Disease relevance of MYOD1


High impact information on MYOD1


Biological context of MYOD1

  • Surprisingly, neither muscle-specific expression, autoregulation, or cross activation depends upon the presence of of these E-box or MEF-2 binding sites in the CMD1 promoter [6].
  • E-box- and MEF-2-independent muscle-specific expression, positive autoregulation, and cross-activation of the chicken MyoD (CMD1) promoter reveal an indirect regulatory pathway [6].
  • CMD1 encodes a polypeptide smaller than MyoD1, 298 versus 318 amino acids, respectively, and is 80% concordant by amino acid sequence overall [5].
  • Specific mutation of the Sp1 site markedly affects transactivation by CMD1 or myogenin [7].
  • Its distal half, containing a pair of E boxes (CANNTG), had been previously characterized as an enhancer responsive to CMD1 but not to c-myogenin [8].

Anatomical context of MYOD1


Associations of MYOD1 with chemical compounds

  • Phosphoinositide turnover under basal conditions in [3H]inositol-labeled cells is faster in myoblasts than in myotubes, a finding that may in part explain the different distribution of PKc observed during the course of myogenic differentiation [11].
  • Gel retardation and methylation interference assays showed that purified CMD1 bound specifically to the mouse muscle creatine kinase enhancer in combination with the in vitro translated E12 [1].
  • Phosphoamino acid of CMD1 from chick primary culture of 11-day embryonic breast muscle was also serine [1].
  • However, CMD1 binding alone is equally efficient when either EDTA is added in excess or dephosphorylated or bacterially expressed CMD1 is used in the assay [12].
  • We also found that myogenin or CMD1 overexpression in chloramphenicol-treated myoblasts did not restore differentiation, thus indicating that an alteration in mitochondrial activity interferes with the ability of myogenic factors to induce terminal differentiation [13].

Other interactions of MYOD1


Analytical, diagnostic and therapeutic context of MYOD1


  1. Possible role of phosphorylation in the function of chicken MyoD1. Nakamura, S. J. Biol. Chem. (1993) [Pubmed]
  2. Beta1 integrin mediation of myogenic differentiation: implications for satellite cell differentiation. Velleman, S.G., McFarland, D.C. Poult. Sci. (2004) [Pubmed]
  3. Preparation of a monoclonal antibody and expression of its antigen associated with myogenic differentiation on spontaneous and artificial myotubes derived from avian myoblasts. Saiuchi, M., Nunoura, N., Kim, J. Cell Struct. Funct. (1993) [Pubmed]
  4. Occupation of the extracellular matrix receptor, integrin, is a control point for myogenic differentiation. Menko, A.S., Boettiger, D. Cell (1987) [Pubmed]
  5. An avian muscle factor related to MyoD1 activates muscle-specific promoters in nonmuscle cells of different germ-layer origin and in BrdU-treated myoblasts. Lin, Z.Y., Dechesne, C.A., Eldridge, J., Paterson, B.M. Genes Dev. (1989) [Pubmed]
  6. E-box- and MEF-2-independent muscle-specific expression, positive autoregulation, and cross-activation of the chicken MyoD (CMD1) promoter reveal an indirect regulatory pathway. Dechesne, C.A., Wei, Q., Eldridge, J., Gannoun-Zaki, L., Millasseau, P., Bougueleret, L., Caterina, D., Paterson, B.M. Mol. Cell. Biol. (1994) [Pubmed]
  7. Muscle-specific expression of the acetylcholine receptor alpha-subunit gene requires both positive and negative interactions between myogenic factors, Sp1 and GBF factors. Bessereau, J.L., Mendelzon, D., LePoupon, C., Fiszman, M., Changeux, J.P., Piette, J. EMBO J. (1993) [Pubmed]
  8. MyoD and myogenin act on the chicken myosin light-chain 1 gene as distinct transcriptional factors. Asakura, A., Fujisawa-Sehara, A., Komiya, T., Nabeshima, Y., Nabeshima, Y. Mol. Cell. Biol. (1993) [Pubmed]
  9. Jun inhibits myogenic differentiation. Su, H.Y., Bos, T.J., Monteclaro, F.S., Vogt, P.K. Oncogene (1991) [Pubmed]
  10. Expression of myogenic differentiation and myotube formation by chick embryo myoblasts in the presence of sodium butyrate. Fiszman, M.Y., Montarras, D., Wright, W., Gros, F. Exp. Cell Res. (1980) [Pubmed]
  11. Activity and regulation of calcium-, phospholipid-dependent protein kinase in differentiating chick myogenic cells. Adamo, S., Caporale, C., Nervi, C., Ceci, R., Molinaro, M. J. Cell Biol. (1989) [Pubmed]
  12. Phosphorylation inhibits the DNA-binding activity of MyoD homodimers but not MyoD-E12 heterodimers. Mitsui, K., Shirakata, M., Paterson, B.M. J. Biol. Chem. (1993) [Pubmed]
  13. Mitochondrial activity is involved in the regulation of myoblast differentiation through myogenin expression and activity of myogenic factors. Rochard, P., Rodier, A., Casas, F., Cassar-Malek, I., Marchal-Victorion, S., Daury, L., Wrutniak, C., Cabello, G. J. Biol. Chem. (2000) [Pubmed]
  14. Effect of TGF-beta 1, TGF-beta 2, and bFGF on chick cartilage and muscle cell differentiation. Schofield, J.N., Wolpert, L. Exp. Cell Res. (1990) [Pubmed]
  15. Differentiation of myogenic cells in micromass cultures of cells from chick facial primordia. Ralphs, J.R., Dhoot, G.K., Tickle, C. Dev. Biol. (1989) [Pubmed]
  16. Multiple effects of interferon on myogenesis in chicken myoblast cultures. Tomita, Y., Hasegawa, S. Biochim. Biophys. Acta (1984) [Pubmed]
  17. Localization of mRNAs coding for CMD1, myogenin and the alpha-subunit of the acetylcholine receptor during skeletal muscle development in the chicken. Piette, J., Huchet, M., Duclert, A., Fujisawa-Sehara, A., Changeux, J.P. Mech. Dev. (1992) [Pubmed]
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