JCB logo
Avanti Polar Lipids, Inc.
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published online
doi:10.1083/jcb.200709019
The Journal of Cell Biology, Vol. 180, No. 6, 1261-1275
The Rockefeller University Press, 0021-9525 $30.00
© Goetz et al.
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 11849K)
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 Goetz, J. G.
Right arrow Articles by Nabi, I. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Goetz, J. G.
Right arrow Articles by Nabi, I. R.
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?

Article

Concerted regulation of focal adhesion dynamics by galectin-3 and tyrosine-phosphorylated caveolin-1



Jacky G. Goetz1,2,3, Bharat Joshi1, Patrick Lajoie1, Scott S. Strugnell1, Trevor Scudamore1, Liliana D. Kojic1, and Ivan R. Nabi1

1 Department of Cellular and Physiological Sciences, Life Sciences Institute, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3
2 Department of Pathology and Cell Biology, University of Montreal, Montreal, Quebec, Canada H3C 3J7
3 LC1 – UMR CNRS 7175, Institut Gilbert Laustriat Pharmacologie et Physico-chimie, Université Louis Pasteur 1, Faculté de Pharmacie, 67401 Illkirch-Graffenstaden Cedex, France

Correspondence to Ivan R. Nabi: ivan.robert.nabi{at}ubc.ca

Both tyrosine-phosphorylated caveolin-1 (pY14Cav1) and GlcNAc-transferase V (Mgat5) are linked with focal adhesions (FAs); however, their function in this context is unknown. Here, we show that galectin-3 binding to Mgat5-modified N-glycans functions together with pY14Cav1 to stabilize focal adhesion kinase (FAK) within FAs, and thereby promotes FA disassembly and turnover. Expression of the Mgat5/galectin lattice alone induces FAs and cell spreading. However, FAK stabilization in FAs also requires expression of pY14Cav1. In cells lacking the Mgat5/galectin lattice, pY14Cav1 is not sufficient to promote FAK stabilization, FA disassembly, and turnover. In human MDA-435 cancer cells, Cav1 expression, but not mutant Y14FCav1, stabilizes FAK exchange and stimulates de novo FA formation in protrusive cellular regions. Thus, transmembrane crosstalk between the galectin lattice and pY14Cav1 promotes FA turnover by stabilizing FAK within FAs defining previously unknown, interdependent roles for galectin-3 and pY14Cav1 in tumor cell migration.

J.G. Goetz's present address is Integrin Signaling Laboratory, Department of Vascular Biology and Inflammation, Centro Nacional de Investigaciones Cardiovasculares (CNIC), 28029 Madrid, Spain.

Abbreviations used in this paper: Cav1, caveolin-1; FA, focal adhesion; FAK, focal adhesion kinase; FN, fibronectin; Gal-3; galectin-3; Mgat5, GlcNAc-transferase V; p, phospho; SW, swainsonine; Y14, tyrosine-14.


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