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J. Biol. Chem., Vol. 277, Issue 6, 4088-4097, February 8, 2002
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From the The transcription factor B-Myb is a cell-cycle
regulated phosphoprotein involved in cell cycle progression through the
transcriptional regulation of many genes. In this study, we show that
the promoter of the fibroblast growth factor-4
(FGF-4) gene is strongly activated by B-Myb in HeLa cells
and it can serve as a novel diagnostic tool for assessing B-Myb
activity. Specifically, B-Myb deletion mutants were examined and
domains of B-Myb required for activation of the FGF-4
promoter were identified. Using phosphorylation-deficient mutant forms
of B-Myb, we also show that phosphorylation is essential for B-Myb
activity. Moreover, a mutant form of B-Myb, which lacks all identified
phosphorylation sites and which has little activity, can function as a
dominant-negative and suppress wild-type B-Myb activity. Acetylation is
another post-translational modification known to affect the activity of
other Myb family members. We show that B-Myb is acetylated by the
co-activator p300. We also show that the bromo and histone
acetyltransferase domains of p300 are sufficient to interact with and
acetylate B-Myb. These data indicate that phosphorylation of B-Myb is
an essential modification for activity and that acetylation of B-Myb
may play a role in B-Myb activity.
Effects of B-Myb on Gene Transcription
PHOSPHORYLATION-DEPENDENT ACTIVITY AND ACETYLATION BY p300*
§,§¶,,§,¶,§**, and§**
Eppley Institute for Research in Cancer and
Allied Diseases, § Department of Pathology and
Microbiology, the ** Department of Biochemistry and
Molecular Biology, University of Nebraska Medical Center,
Omaha, Nebraska 68198-6805
*
This work was supported in part by National Institutes of
Health NCI Grants CA74771 (to A. R.) and CA79491 (to A. R.),
American Cancer Society Grant BE-260 (to R. L.), and core
facilities of the University of Nebraska Medical Center Eppley Cancer
Center used in the course of this work were supported in part by
National Institutes of Health NCI Laboratory Cancer Research Support
Grant CA36727.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Eppley Cancer
Institute, University of Nebraska Medical Center, 986805 Nebraska Medical Center, Omaha, NE 68198-6805. Tel.: 402-559-6338; Fax: 402-559-4651; E-mail: arizzino@unmc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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