JCB logo
TILL Photonics: www.till-photonics.com
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 14 April 2003. doi:10.1083/jcb.200211015
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 325K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
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 Garvalov, B. K.
Right arrow Articles by Way, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Garvalov, B. K.
Right arrow Articles by Way, M.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© The Rockefeller University Press, 0021-9525/2003/4/33 $5.00
The Journal of Cell Biology, Volume 161, Number 1, 33-39

Report

The conformational state of Tes regulates its zyxin-dependent recruitment to focal adhesions



Boyan K. Garvalov1, Theresa E. Higgins2, James D. Sutherland2, Markus Zettl2, Niki Scaplehorn2, Thomas Köcher1, Eugenia Piddini1, Gareth Griffiths1 and Michael Way1,2

1 European Molecular Biology Laboratory, D-69117 Heidelberg, Germany
2 Cell Motility Laboratory, Cancer Research UK, Lincoln's Inn Fields Laboratories, London, WC2A 3PX UK

Address correspondence to Michael Way, Cell Motility Laboratory, Cancer Research UK, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London, WC2A 3PX UK. Tel.: 44-207-269-3733. Fax: 44-207-269-3581. E-mail: michael.way{at}cancer.org.uk

The function of the human Tes protein, which has extensive similarity to zyxin in both sequence and domain organization, is currently unknown. We now show that Tes is a component of focal adhesions that, when expressed, negatively regulates proliferation of T47D breast carcinoma cells. Coimmunoprecipitations demonstrate that in vivo Tes is complexed with actin, Mena, and vasodilator-stimulated phosphoprotein (VASP). Interestingly, the isolated NH2-terminal half of Tes pulls out {alpha}-actinin and paxillin from cell extracts in addition to actin. The COOH-terminal half recruits zyxin as well as Mena and VASP from cell extracts. These differences suggest that the ability of Tes to associate with {alpha}-actinin, paxillin, and zyxin is dependent on the conformational state of the molecule. Consistent with this hypothesis, we demonstrate that the two halves of Tes interact with each other in vitro and in vivo. Using fibroblasts lacking Mena and VASP, we show that these proteins are not required to recruit Tes to focal adhesions. However, using RNAi ablation, we demonstrate that zyxin is required to recruit Tes, as well as Mena and VASP, but not vinculin or paxillin, to focal adhesions.

Key Words: Tes; focal adhesion; zyxin; RNAi; conformation

The online version of this article includes supplemental material.

* Abbreviation used in this paper: VASP, vasodilator-stimulated phosphoprotein.


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 Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:



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