Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article Full Text Full Text (PDF, 3923K) PDF+supp data (6490K) PPT slides of all figures Supplemental Material Alert me when this article is cited Citation Map Services Email this article Similar articles in this journal Similar articles in PubMed Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Google Scholar Articles by Maher, M. T. Articles by Gottardi, C. J. PubMed PubMed Citation Articles by Maher, M. T. Articles by Gottardi, C. J. Related Collections Related Article Related In this Issue article Social Bookmarking                            What's this?

Activity of the β-catenin phosphodestruction complex at cell–cell contacts is enhanced by cadherin-based adhesion

¹ Department of Medicine, ² Integrated Graduate Program in the Life Sciences, ³ Department of Pathology, and ⁴ Robert H. Lurie Comprehensive Cancer Center, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611

Correspondence to Cara J. Gottardi: c-gottardi{at}northwestern.edu

It is well established that cadherin protein levels impact canonical Wnt signaling through binding and sequestering β-catenin (β-cat) from T-cell factor family transcription factors. Whether changes in intercellular adhesion can affect β-cat signaling and the mechanism through which this occurs has remained unresolved. We show that axin, APC2, GSK-3β and N-terminally phosphorylated forms of β-cat can localize to cell–cell contacts in a complex that is molecularly distinct from the cadherin–catenin adhesive complex. Nonetheless, cadherins can promote the N-terminal phosphorylation of β-cat, and cell–cell adhesion increases the turnover of cytosolic β-cat. Together, these data suggest that cadherin-based cell–cell adhesion limits Wnt signals by promoting the activity of a junction-localized β-cat phosphodestruction complex, which may be relevant to tissue morphogenesis and cell fate decisions during development.

© 2009 Maher et al.
This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

CiteULike

Complore

Connotea

Del.icio.us

Digg

Facebook

Reddit

Technorati

Twitter

This article has been cited by other articles:

• Mo, R., Chew, T.-L., Maher, M. T., Bellipanni, G., Weinberg, E. S., Gottardi, C. J. (2009). The Terminal Region of {beta}-Catenin Promotes Stability by Shielding the Armadillo Repeats from the Axin-scaffold Destruction Complex. J. Biol. Chem. 284: 28222-28231 [Abstract] [Full Text]  
• Leslie, M. (2009). Killing the {beta}-catenin messenger. JCB 186: 164-164 [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents