The Role of E-Cadherin, catenin p120ctn, and Hakai in Cell Motility

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P120CAS is an armadillo-type catenin which in 3T3 fibroblasts induces marked extensions of cellular processes and increased cell motility. Deletion of the p120CAS- binding site of E-cadherin induces similarly increased motility in cells. Gene ablation of p120CAS in the mouse resulted in an arrest of development at E8.75: homozygous mutant embryos do not turn and show a defective notochord, accompanied by dramatic overexpression of the neural ectoderm. This is a surprising phenotype which requires further work to elucidate the role of p120CAS in cell motility, cell adhesion and signalling in vivo. Moreover, conditional gene ablations will be performed to examine the role of p120CAS at later stages of embryogenesis and in the adult. We have also found new interaction partners for the tyrosinephosphorylated p120CAS binding site of E-cadherin, among them E7, a component with structural homology to c-cbl. E7 could play a role in degradation of E-cadherin or interfere with p120CAS function. The interrelationship of E-cadherin with p120CAS and the c-cbl homolog in cell motility will be examined.