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

Nature volume 344, pages 517–522 (1990)Cite this article

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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Authors and Affiliations

  1. Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1124 Columbia Street, Seattle, Washington, 98104, USA

    Bernhard Lüscher, Erik Christenson & Robert N. Eisenman

  2. Howard Hughes Medical Institute, University of Washington, School of Medicine, Seattle, Washington, 98195, USA

    David W. Litchfield & Edwin G. Krebs

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  1. Bernhard Lüscher
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  2. Erik Christenson
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  3. David W. Litchfield
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  4. Edwin G. Krebs
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  5. Robert N. Eisenman
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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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