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J. Biol. Chem., Vol. 277, Issue 35, 31694-31702, August 30, 2002
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From the YB-1 is a member of the cold shock domain family
of proteins that is important for signaling DNA damage and cell
proliferation. YB-1 is induced by DNA damage and can also recognize
cisplatin-modified DNA. In this study we observed a 6-fold increase in
the steady-state level of YB-1 mRNA in response to cisplatin
exposure in cells of the human cancer cell line KB. We present evidence
from cotransfection experiments for a critical role of c-Myc and p73 in
the transactivation of the YB-1 promoter. p73 transactivated the YB-1
promoter in experiments with Saos-2 cells, which express c-Myc, but not
with HO15.19 cells, which lack c-Myc. In turn, c-Myc transactivated an
intact YB-1 promoter but not a YB-1 promoter with a mutant E-box,
indicating that the E-box is necessary for the response of the promoter
to cisplatin. We also found that p73 interacts with c-Myc in
vitro and in vivo. Using deletion mutants we showed that the DNA-binding domain of p73 and the C-terminal region of c-Myc
are required for the interaction. Furthermore, p73 stimulated the
interaction of Max with c-Myc and promoted binding of the c-Myc-Max
complex to its target DNA. Our data suggest that p73 stimulates the
transcription of the YB-1 promoter by enhancing recruitment of the
c-Myc-Max complex to the E-box.
p73 Interacts with c-Myc to Regulate Y-box-binding Protein-1
Expression*
,,,
,
Department of Molecular Biology, University
of Occupational and Environmental Health, Yahatanishi-ku, Kitakyushu
807-8555, Japan, the § Institute for Genetic Medicine,
Hokkaido University, Kita-15, Nishi-7, Kita-ku, Sapporo 060-0815, Japan, the ¶ Department of Medical Biochemistry, Graduate School
of Medical Sciences, Kyushu University, Higashi-ku, Fukuoka
812-8582, Japan, the Department of Surgery II, University of
Occupational and Environmental Health, Yahatanishi-ku, Kitakyushu
807-8555, Japan, and the ** Department of Cell Biology,
Institute of Anatomy and Cell Biology, Göteborg University,
SE-405 30, Gothenburg, Sweden
*
This work was supported in part by a grant-in-aid for Cancer
Research from the Ministry of Education, Science, Sports, and Culture
of Japan, by Research Grant 99-23106 from the Princess Takamatsu Cancer
Research Fund, and by a grant from the Fukuoka Anticancer Research
Fund, as well as by grants from the Swedish Cancer Foundation, the
Childhood Cancer Foundation, and the Ingabritt and Arne Lundberg
Foundation.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: Dept. of Molecular
Biology, University of Occupational and Environmental Health, 1-1 Iseigaoka, Yahatanishi-ku, Kitakyushu 807-8555, Japan. Tel.: 81-93-691-7423; Fax: 81-93-692-2766; E-mail:
k-kohno@med.uoeh-u.ac.jp.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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