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© The Rockefeller University Press, 0021-9525/1999//551 $5.00
The Journal of Cell Biology, Volume 145, Number 3, , 1999 551-562

p120^ctn Acts as an Inhibitory Regulator of Cadherin Function in Colon Carcinoma Cells

Shinya Aono^*, Shinichi Nakagawa^*, Albert B. Reynolds, and Masatoshi Takeichi^*

^* Department of Biophysics, Faculty of Science, Kyoto University, Kyoto 606-8502, Japan; and Department of Cell Biology, Vanderbilt University, School of Medicine, Nashville, Tennessee 37232-2175

p120^ctn binds to the cytoplasmic domain of cadherins but its role is poorly understood. Colo 205 cells grow as dispersed cells despite their normal expression of E-cadherin and catenins. However, in these cells we can induce typical E-cadherin–dependent aggregation by treatment with staurosporine or trypsin. These treatments concomitantly induce an electrophoretic mobility shift of p120^ctn to a faster position. To investigate whether p120^ctn plays a role in this cadherin reactivation process, we transfected Colo 205 cells with a series of p120^ctn deletion constructs. Notably, expression of NH₂-terminally deleted p120^ctn induced aggregation. Similar effects were observed when these constructs were introduced into HT-29 cells. When a mutant N-cadherin lacking the p120^ctn-binding site was introduced into Colo 205 cells, this molecule also induced cell aggregation, indicating that cadherins can function normally if they do not bind to p120^ctn. These findings suggest that in Colo 205 cells, a signaling mechanism exists to modify a biochemical state of p120^ctn and the modified p120^ctn blocks the cadherin system. The NH₂ terminus–deleted p120^ctn appears to compete with the endogenous p120^ctn to abolish the adhesion-blocking action.

Key Words: E-cadherin • catenin • colon carcinoma • Colo 205 • p120^ctn

Abbreviations used in this paper: aa, amino acid; FLf, full-length FLAG-tagged p120^ctn.

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