Myb DNA binding inhibited by phosphorylation at a site deleted during oncogenic activation |
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Authors: | B Lüscher E Christenson D W Litchfield E G Krebs R N Eisenman |
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Affiliation: | Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98104. |
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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-II-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 independent 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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