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First published online June 28, 2004

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Cadherin-catenin connections

Cadherins are membrane proteins that mediate adhesion between cells. They are linked to the actin cytoskeleton through ß- and -catenin. This is essential for adhesion and appears to depend on dephosphorylation of Tyr564 of ß-catenin, which allows it to interact with the cadherin cytoplasmic domain. The phosphatase responsible seems to be PTP1B, but how this is controlled has been unclear. Jack Lilien and co-workers now reveal that a tyrosine kinase, Fer, is the key (see p. 3207). They show that Fer is brought into the cadherin complex by another catenin – p120. If the p120-Fer interaction is disrupted, Fer leaves the complex, as do PTP1B and ß-catenin (which has become phosphorylated), and cells no longer adhere. Significantly, when the authors mutate Tyr564 of ß-catenin, the cadherin complex remains intact even in the absence of Fer. Lilien and co-workers go on to demonstrate that Fer phosphorylates PTP1B and that the cadherin-catenin-PTP1B complex is disrupted in cells from mice lacking active Fer. They conclude that phosphorylation of PTP1B by Fer is essential to keep the phosphatase associated with the cadherin-catenin complex so that it can dephosphorylate ß-catenin and thereby maintain cell-cell adhesion.

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Related articles in JCS:

Continuous association of cadherin with ß-catenin requires the non-receptor tyrosine-kinase Fer

Gang Xu, Andrew W. B. Craig, Peter Greer, Matthew Miller, Panos Z. Anastasiadis, Jack Lilien, and Janne Balsamo
JCS 2004 117: 3207-3219. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?