Abstract
The c-Myb nuclear oncoprotein is phosphorylated in vitro and in vivo at an N-terminal site near its DNA-binding domain by casein kinase II (CK-II) or a CK-ll-like activity. This in vitro phosphorylation reversibly inhibits the sequence-specific binding of c-Myb to DNA. The site of this phosphorylation is deleted in nearly all oncogenically activated Myb proteins, resulting in DNA-binding that is indepen-dent of CK-II. Because CK-II activity is modulated by growth factors, loss of the site could uncouple c-Myb from its normal physiological regulator.
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Lüscher, B., Christenson, E., Litchfield, D. et al. Myb DNA binding inhibited by phosphorylation at a site deleted during oncogenic activation. Nature 344, 517–522 (1990). https://doi.org/10.1038/344517a0
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DOI: https://doi.org/10.1038/344517a0
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