JCB logo
PeproTech: Cell Culture Supplements
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 10 May 2004. doi:10.1083/jcb1653iti5
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 165, Number 3, 295-295
This Article
Right arrow Full Text (PDF, 618K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wells, W. A.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Wells, W. A.
Related Collections
Right arrowRelated Article
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?

In This Issue

Sensing detachment


Cells lacking vinculin survive after detachment because they phosphorylate ERK.

Teasing apart the contributions of so many motility proteins has proven difficult. So Subauste et al. report in this issue that they turned to an all-or-none readout—apoptotic cell death—to answer some of the same questions (page 371). They find that the attachment and motility protein vinculin pokes its nose between paxillin and FAK, thus disrupting signal transduction that activates the survival signals sent by extracellular signal–related kinase (ERK).

After serum withdrawal, detachment from a substrate, or pro-apoptotic drug treatment, cells lacking vinculin were compared with wild-type cells. The cells lacking vinculin showed greater paxillin–FAK interaction, an increase in ERK phosphorylation, and reduced apoptosis.

The reduction in apoptosis (and increase in migration rates) could be reversed by ERK pathway inhibitors. This is reminiscent of the behavior of many cancer cell lines, which lack vinculin and are extremely metastatic and motile unless vinculin expression is restored.

Wild-type cells may survive when attached because of low level ERK signaling. That signaling must be repressed after detachment, in part via the interfering actions of vinculin. Cells lacking vinculin send an excess of the survival signal and thus fail to make the correct change in both their attachment structures and signaling pathways in response to the new nonadherent situation. {blacksquare}



William A. Wells

wellsw{at}rockefeller.edu


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?

Related Article

Vinculin modulation of paxillin–FAK interactions regulates ERK to control survival and motility
M. Cecilia Subauste, Olivier Pertz, Eileen D. Adamson, Christopher E. Turner, Sachiko Junger, and Klaus M. Hahn
J. Cell Biol. 2004 165: 371-381. [Abstract] [Full Text] [PDF]




This Article
Right arrow Full Text (PDF, 618K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wells, W. A.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Wells, W. A.
Related Collections
Right arrowRelated Article
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?

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