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Vol. 19, Issue 10, 4042-4050, October 2008

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p120-Catenin Is a Key Component of the Cadherin–-Secretase Supercomplex

Alexi Kiss^*, Regina B. Troyanovsky, and Sergey M. Troyanovsky

*Division of Dermatology, Washington University Medical School, St. Louis, MO 63110; and Department of Dermatology, Northwestern University, The Feinberg School of Medicine, Chicago, IL 60611

Submitted April 17, 2008; Revised June 17, 2008; Accepted July 7, 2008
Monitoring Editor: Asma Nusrat

In this work, we show several previously unknown features of p120-catenin in a cadherin–catenin complex that are critical for our understanding of cadherin-based adhesion and signaling. We show that in human epithelial A-431 cells, nearly all p120 molecules engage in high-affinity interaction with E-cadherin–catenin complexes located at the cellular surface. p120 is positioned in proximity to -catenin in the complex with cadherin. These findings suggest a functional cooperation between p120 and -catenin in cadherin-based adhesion. A low level of cadherin-free p120 molecules, in contrast, could facilitate p120-dependent signaling. Finally, we present compelling evidence that p120 is a key linker cementing the E-cadherin–catenin complex with the transmembrane protease -secretase. The cell–cell contact location of this supercomplex makes it an important candidate for conducting different signals that rely on -secretase proteolytic activity.

Address correspondence to: Sergey Troyanovsky (s-troyanovsky{at}northwestern.edu)