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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Two putative protein kinase CK2 phosphorylation sites are important for Myf-5 activity.

Myf-5, a member of a family of muscle-specific transcription factors, is important for myogenic cell determination and differentiation. Here, we report that Myf-5 protein constitutes a substrate for phosphorylation in vitro by protein kinase CK2. We identified two potential phosphorylation sites at serine49 and serine133, both of which seem to be necessary for Myf-5 activity. Mutants which can no longer be phosphorylated fail to transactivate E-box-dependent reporter genes and act as trans-dominant repressors of wild-type Myf-5. Normal activity can be restored by replacing the serine residues with glutamate suggesting that a negative charge at these sites is obligatory for Myf-5 activity. Although serine133 is part of helix 2 which mediates dimerization, we find no evidence for impaired DNA-binding or heterodimerization of the Ser-Ala133 mutant. Some serine49 mutations exhibit reduced nuclear localization and/or protein stability. Our data suggest that CK2-mediated phosphorylation of Myf-5 is required for Myf-5 activity.[1]


  1. Two putative protein kinase CK2 phosphorylation sites are important for Myf-5 activity. Winter, B., Kautzner, I., Issinger, O.G., Arnold, H.H. Biol. Chem. (1997) [Pubmed]
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