JCB logo
R&D Systems: New Poster Available
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 536K)
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 Weiss, E. E.
Right arrow Articles by Rüdiger, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Weiss, E. E.
Right arrow Articles by Rüdiger, 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, 0021-9525/1998//755 $5.00
The Journal of Cell Biology, Volume 141, Number 3, , 1998 755-764

Articles

Vinculin Is Part of the Cadherin–Catenin Junctional Complex: Complex Formation between {alpha}-Catenin and Vinculin



Elisabeth E. Weiss*, Martina Kroemker*, Angelika-H. Rüdiger{ddagger}, Brigitte M. Jockusch*, and Manfred Rüdiger*

* Cell Biology, Zoological Institute, Technical University, 38092 Braunschweig, Germany; and {ddagger} Division of Cell Biology and Immunology, National Research Centre for Biotechnology, 38124 Braunschweig, Germany

In epithelial cells, {alpha}-, β-, and {gamma}-catenin are involved in linking the peripheral microfilament belt to the transmembrane protein E-cadherin. {alpha}-Catenin exhibits sequence homologies over three regions to vinculin, another adherens junction protein. While vinculin is found in cell–matrix and cell–cell contacts, {alpha}-catenin is restricted to the latter. To elucidate, whether vinculin is part of the cell–cell junctional complex, we investigated complex formation and intracellular targeting of vinculin and {alpha}-catenin. We show that {alpha}-catenin colocalizes at cell–cell contacts with endogenous vinculin and also with the transfected vinculin head domain forming immunoprecipitable complexes. In vitro, the vinculin NH2-terminal head binds to {alpha}-catenin, as seen by immunoprecipitation, dot overlay, cosedimentation, and surface plasmon resonance measurements. The Kd of the complex was determined to 2–4 x 10–7 M. As seen by overlays and affinity mass spectrometry, the COOH-terminal region of {alpha}-catenin is involved in this interaction.

Complex formation of vinculin and {alpha}-catenin was challenged in transfected cells. In PtK2 cells, intact {alpha}-catenin and {alpha}-catenin1-670, harboring the β-catenin– binding site, were directed to cell–cell contacts. In contrast, {alpha}-catenin697–906 fragments were recruited to cell–cell contacts, focal adhesions, and stress fibers. Our results imply that in vivo {alpha}-catenin, like vinculin, is tightly regulated in its ligand binding activity.

Abbreviations used in this paper: DFP, diisopropylfluorophosphate; DSP, dithiobis(succinimidylproppionate); MDBK, Madin–Darby bovine kidney epithelial cells; PIP2, phosphatidylinositol-4,5-bisphosphate; PtK2, Potourus tridactylus kidney epithelial cells; RU, resonance units.

Address all correspondence to Dr. Manfred Rüdiger, Cell Biology, Zoological Institute, Technical University Braunschweig, 38092 Braunschweig, Germany. Tel.: 0531-391-3191. Fax: 0531-391-8203. E-mail: m.ruediger{at}tu-bs.de


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