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A more recent version of this article appeared on January 11, 2002
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M110248200v1
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Papers In Press, published online ahead of print November 15, 2001
J. Biol. Chem, 10.1074/jbc.M110248200
Submitted on October 24, 2001
Revised on November 15, 2001
Accepted on November 15, 2001

The transcriptional factor Tcf-4 contains different binding sites for beta-catenin and plakoglobin

Susana Miravet, Jose Piedra, Francesc Miro, Emilio Itarte, Antonio Garcia de Herreros, and Mireia Dunach

Department of Biochemistry and Molecular Biology, Universitat Autonoma de Barcelona, 08193, Bellaterra

Corresponding Author: mireia.dunach{at}uab.es

beta -catenin and plakoglobin are two related armadillo proteins necessary for the establishment of adhesion junctions and desmosomes. Moreover, beta -catenin can also act as a transcriptional co-activator through its interaction with the members of Tcf/LEF-1 transcriptional factor family. We show here that Tcf-4 can be phosphorylated in vitro by protein kinase CK2 stoichiometrically in aminoacids Ser58-Ser59-Ser60. Phosphorylation of these residues does not modify the interaction of Tcf-4 with beta -catenin but reduces its association to plakoglobin. The binding sites of Tcf-4 for these two proteins were compared: whereas beta -catenin requires the amino-terminal first 50 aminoacids, plakoglobin interacts mainly with residues 51-80. Tcf-4 (51-80) binds plakoglobin in the region of armadillo repeats 1-6. Ternary complexes composed by beta -catenin/Tcf-4/plakoglobin could be detected in vitro, demonstrating that simultaneous binding of the two armadillo proteins to Tcf-4 is possible. Experiments performed using a Tcf-4 mutant with decreased interaction to plakoglobin demonstrated that binding to this protein negatively affected the transcriptional activity of Tcf-4. These results indicate that Tcf-4 contains two different sites for binding of beta -catenin and plakoglobin and the interaction of the latter hinders the transcriptional activity of the complex.


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