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Myb DNA binding inhibited by phosphorylation at a site deleted during oncogenic activation.

Lüscher, B and Christenson, E and Litchfield, D W and Krebs, E G and Eisenman, R N (1990) Myb DNA binding inhibited by phosphorylation at a site deleted during oncogenic activation. Nature, 344 (6266). pp. 517-522. ISSN 0028-0836

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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.

Item Type: Article
Additional Information: This article is available to Nature subscribers only at the link above.
DOI: 10.1038/344517a0
PubMed ID: 2157164
Keywords or MeSH Headings: Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Binding, Competitive; Casein Kinases; Cell Line; Chickens; DNA-Binding Proteins/metabolism; Immunosorbent Techniques; Leukemia Virus, Murine/genetics; Leukemia, Experimental/metabolism; Molecular Sequence Data; Oncogenes; Phosphorylation; Protein Kinases/metabolism; Proto-Oncogene Proteins/metabolism; Proto-Oncogene Proteins c-myb; Tumor Cells, Cultured;
Subjects: Molecules > Molecular structure
Molecules > Proteins
Molecules > Genes > Oncogenes
Depositing User: Library Staff
Date Deposited: 03 Dec 2008 22:13
Last Modified: 21 May 2010 22:45

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