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J. Biol. Chem., Vol. 276, Issue 25, 22699-22708, June 22, 2001
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From the Department of Molecular Cancer Biology, Institute of
Cancer Biology, Danish Cancer Society, Strandboulevarden 49, DK-2100
Copenhagen Ø, Denmark and A physical and functional interaction between the
Ca2+-binding protein Mts1 (S100A4) and the tumor
suppressor p53 protein is shown here for the first time. We demonstrate
that Mts1 binds to the extreme end of the C-terminal regulatory domain
of p53 by several in vitro and in vivo
approaches: co-immunoprecipitation, affinity chromatography, and far
Western blot analysis. The Mts1 protein in vitro inhibits
phosphorylation of the full-length p53 and its C-terminal peptide by
protein kinase C but not by casein kinase II. The Mts1 binding
to p53 interferes with the DNA binding activity of p53 in
vitro and reporter gene transactivation in vivo, and
this has a regulatory function. A differential modulation of the p53
target gene (p21/WAF, bax, thrombospondin-1,
and mdm-2) transcription was observed upon Mts1
induction in tet-inducible cell lines expressing wild type
p53. Mts1 cooperates with wild type p53 in apoptosis induction. Our
data imply that the ability of Mts1 to enhance
p53-dependent apoptosis might accelerate the loss of wild
type p53 function in tumors. In this way, Mts1 can contribute to the
development of a more aggressive phenotype during tumor progression.
Tumor Suppressor p53 Protein Is a New Target for
the Metastasis-associated Mts1/S100A4 Protein
FUNCTIONAL CONSEQUENCES OF THEIR INTERACTION*
,
, and Microbiology and Tumor Biology
Center, Karolinska Institute, SE-171 77 Stockholm, Sweden
*
This study was supported by Grants from the Danish Cancer
Society, INTAS, Novo Nordisc Foundation, Dansk Kræftforsknings
Fond, and Danish Medical Research Council.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. Tel.: 45-35-25-73-13;
Fax: 45-35-25-77-21; E-mail: mg@cancer.dk.
§
Present address: Dept. of Biosciences at Novum, Karolinska
Institutet SE-141 57 Huddinge, Sweden.
¶
Present address: Dana Faber Cancer Institute and Harvard
Medical School, 44 Binney St., Boston, MA 02115.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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