Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Sci. STKE, 15 August 2000
Vol. 2000, Issue 45, p. tw4
[DOI: 10.1126/stke.2000.45.tw4]


Cell Biology The p120 Catenin Shuffle

It has not been clear how the cytoplasmic protein p120 catenin regulates cell motility. Overexpression of p120 catenin in fibroblasts modulates the actin cytoskeleton and promotes cell motility, yet binding to the cytoplasmic domain of coexpresssed cadherins, cell surface adhesion proteins, inhibits this effect. Noren et al. now report that, when in the cytoplasm, p120 catenin binds to Vav2, an exchange factor that activates Cdc42 and Rac1. These small GTP-binding proteins alter the actin cytoskeleton and promote cell motility. However, the presence of cadherins can cause a decrease in the availability of cytoplasmic p120 and thus inhibit cell migration and promote cell-cell adhesion. The authors suggest that the distribution of p120 catenin between the cadherin-bound state and the cytoplasmic pool is important in determining cell motility.

Noren, N.K., Liu, B.P., Burridge, K., and Kreft, B. (2000) p120 catenin regulates the actin cytoskeleton via Rho family GTPases. J. Cell Biol. 150: 567-579. [Abstract] [Full Text]

Citation: The p120 Catenin Shuffle. Sci. STKE 2000, tw4 (2000).

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882