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Molecular and Cellular Biology, April 2003, p. 2287-2297, Vol. 23, No. 7
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.7.2287-2297.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

p120 Catenin-Associated Fer and Fyn Tyrosine Kinases Regulate ß-Catenin Tyr-142 Phosphorylation and ß-Catenin-{alpha}-Catenin Interaction

Jose Piedra,1,2 Susana Miravet,1 Julio Castaño,1 Héctor G. Pálmer,3 Nora Heisterkamp,4 Antonio García de Herreros,2* and Mireia Duñach1*

Unitat de Biofísica, Departament de Bioquímica i Biologia Molecular, Facultat de Medicina, Universitat Autònoma de Barcelona, E-08193 Bellaterra,1 Unitat de Biologia Cel·lular i Molecular, Institut Municipal d'Investigació Mèdica, Universitat Pompeu Fabra, E-08003 Barcelona,2 Instituto de Investigaciones Biomédicas "Alberto Sols," CSIC-Universidad Autónoma de Madrid, E-28029 Madrid, Spain,3 Department of Pathology, Children's Hospital of Los Angeles Research Institute and School of Medicine, University of Southern California, Los Angeles, California 900274

Received 21 October 2002/ Returned for modification 21 November 2002/ Accepted 2 January 2003

ß-Catenin has a key role in the formation of adherens junction through its interactions with E-cadherin and {alpha}-catenin. We show here that interaction of ß-catenin with {alpha}-catenin is regulated by the phosphorylation of ß-catenin Tyr-142. This residue can be phosphorylated in vitro by Fer or Fyn tyrosine kinases. Transfection of these kinases to epithelial cells disrupted the association between both catenins. We have also examined whether these kinases are involved in the regulation of this interaction by K-ras. Stable transfectants of the K-ras oncogene in intestinal epithelial IEC18 cells were generated which show little {alpha}-catenin-ß-catenin association with respect to control clones; this effect is accompanied by increased Tyr-142 phosphorylation and activation of Fer and Fyn kinases. As reported for Fer, Fyn kinase is constitutively bound to p120 catenin; expression of K-ras induces the phosphorylation of p120 catenin on tyrosine residues increasing its affinity for E-cadherin and, consequently, promotes the association of Fyn with the adherens junction complex. Yes tyrosine kinase also binds to p120 catenin but only upon activation, and stimulates Fer and Fyn tyrosine kinases. These results indicate that p120 catenin acts as a docking protein facilitating the activation of Fer/Fyn tyrosine kinases by Yes and demonstrate the role of these p120 catenin-associated kinases in the regulation of ß-catenin-{alpha}-catenin interaction.

* Corresponding author. Mailing address for Mireia Duñach: Unitat de Biofísica, Departament Bioquímica i Biologia Molecular, Facultat de Medicina, Universitat Autònoma de Barcelona, E-08193 Bellaterra, Spain. Phone: 34-93-581-1870. Fax: 34-93-581-1907. E-mail: mireia.dunach{at}uab.es. Mailing address for Antonio García de Herreros: Institut Municipal d'Investigació Mèdica, c/Dr. Aiguader 80, E-08003 Barcelona, Spain. Phone: 34-93-221-1009. Fax: 34-93-221-3237. E-mail: agarcia{at}imim.es.

Molecular and Cellular Biology, April 2003, p. 2287-2297, Vol. 23, No. 7
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.7.2287-2297.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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