JCB logo
Avanti Polar Lipids, Inc.
  Home | Help | Feedback | Subscriptions | Archive | Search | Latest Articles
Published online 27 January 2003. doi:10.1083/jcb.200207160
 The Rockefeller University Press, 0021-9525 $8.00
The Journal of Cell Biology
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 2107K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pacquelet, A.
Right arrow Articles by Rørth, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pacquelet, A.
Right arrow Articles by Rørth, P.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

© The Rockefeller University Press, 0021-9525
The Journal of Cell Biology

Report

Binding site for p120/{delta}-catenin is not required for Drosophila E-cadherin function in vivo



Anne Pacquelet, Li Lin and Pernille Rørth

European Molecular Biology Laboratory, 69117 Heidelberg, Germany

Address correspondence to Pernille Rørth, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany. Tel.: 49 6221 387109. Fax: 49 6221 387166. E-mail: rorth{at}EMBL-Heidelberg.de

Homophilic cell adhesion mediated by classical cadherins is important for many developmental processes. Proteins that interact with the cytoplasmic domain of cadherin, in particular the catenins, are thought to regulate the strength and possibly the dynamics of adhesion. ß-catenin links cadherin to the actin cytoskeleton via {alpha}-catenin. The role of p120/{delta}-catenin proteins in regulating cadherin function is less clear. Both ß-catenin and p120/{delta}-catenin are conserved in Drosophila. Here, we address the importance of cadherin–catenin interactions in vivo, using mutant variants of Drosophila epithelial cadherin (DE-cadherin) that are selectively defective in p120ctn (DE-cadherin-AAA) or ß-catenin–armadillo (DE-cadherin-{Delta}ß) interactions. We have analyzed the ability of these proteins to substitute for endogenous DE-cadherin activity in multiple cadherin-dependent processes during Drosophila development and oogenesis; epithelial integrity, follicle cell sorting, oocyte positioning, as well as the dynamic adhesion required for border cell migration. As expected, DE-cadherin-{Delta}ß did not substitute for DE-cadherin in these processes, although it retained some residual activity. Surprisingly, DE-cadherin-AAA was able to substitute for the wild-type protein in all contexts with no detectable perturbations. Thus, interaction with p120/{delta}-catenin does not appear to be required for DE-cadherin function in vivo.

Key Words: cell adhesion; oogenesis; migration; morphogenesis; adherens junction


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Latest Articles