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, 468K)
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 Nix, D. A.
Right arrow Articles by Beckerle, M. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nix, D. A.
Right arrow Articles by Beckerle, M. C.
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, 0021-9525/1997//1139 $5.00
The Journal of Cell Biology, Volume 138, Number 5, , 1997 1139-1147

Article

Nuclear–Cytoplasmic Shuttling of the Focal Contact Protein, Zyxin: A Potential Mechanism for Communication between Sites of Cell Adhesion and the Nucleus



David A. Nix and Mary C. Beckerle

Department of Biology, University of Utah, Salt Lake City, Utah 84112

Integrin-dependent cell adhesion to specific extracellular matrix molecules has been demonstrated to trigger dramatic changes in gene expression that can affect cell fate. However, little is understood about the molecular mechanism by which events at sites of cell– substratum adhesion are communicated to the cell interior to regulate the transcriptional apparatus. By analogy to classical mechanisms of cell surface receptor function, it seems likely that some components of the integrin-activated signal transduction machinery will be colocalized with cell adhesion molecules. Zyxin is a low abundance phosphoprotein that accumulates with integrins at sites of cell–substratum attachment. Here we show that zyxin exhibits a functional nuclear export signal that is required to keep zyxin concentrated in the cytoplasm and is sufficient to direct nuclear proteins to the cytosol. Furthermore, we demonstrate that native zyxin shuttles between the nucleus and sites of cell adhesion in fibroblasts and is thus an excellent candidate for relaying information between these two compartments.

Abbreviations used in this paper: β-gal, β-galactosidase; GST, glutathione-S-transferase; NES, nuclear export signal.

Please address all correspondence to Mary C. Beckerle, Department of Biology, 201 South Biology Building, University of Utah, Salt Lake City, UT 84112-0840. Tel.: (801) 581-4485; Fax: (801) 581-4668; E-mail: beckerle @bioscience.utah.edu

The authors are particularly grateful to S. Tsukita for the anti-zyxin monoclonal antibody, to D. Gard and B. Stronach for helpful suggestions, and to K. Schmeichel for help with Fig. 7.

This research was supported by National Institutes of Health predoctoral award to D.A. Nix (CA09602) and by a National Institutes of Health grant (GM50877) to M.C. Beckerle. M.C. Beckerle is a recipient of a Faculty Research Award from the American Cancer Society. Support from the University of Utah Sequencing Facility and Biotechnology Core Facility (CA42014) is also gratefully acknowledged.


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