spacer gif spacer gif spacer gif spacer gif The Node. Discuss debate and deliberate developmental biology spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online 10 November 2009
doi: 10.1242/jcs.055996

Journal of Cell Science 122, 4363-4374 (2009)
Published by The Company of Biologists 2009
This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Material
Right arrow All Versions of this Article:
jcs.055996v1
122/23/4363    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Related articles in JCS
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Delon, I.
Right arrow Articles by Brown, N. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Delon, I.
Right arrow Articles by Brown, N. H.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Research Article

The integrin adhesion complex changes its composition and function during morphogenesis of an epithelium

Isabelle Delon and Nicholas H. Brown*

Gurdon Institute and Department of Physiology, Development and Neuroscience, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK

* Author for correspondence (n.brown{at}gurdon.cam.ac.uk)

Accepted 8 October 2009

Cell adhesion to the extracellular matrix (ECM) is mediated by the integrin family of transmembrane receptors. Integrins link ECM ligands to the cytoskeleton, providing strong attachment to enable cell-shape change and tissue integrity. This connection is made possible by an intracellular complex of proteins, which links to actin filaments and controls signalling cascades that regulate cytoskeletal rearrangements. We have identified stress-fibre-associated focal adhesions that change their composition during tissue morphogenesis. Early expression of {alpha}PS1βPS integrin decreases the levels of the actin-nucleating factors Enabled, Diaphanous and profilin, as well as downregulating the amount of F-actin incorporated into the stress fibres. As follicle cells mature in their developmental pathway and become squamous, the integrin in the focal adhesions changes from {alpha}PS1βPS to {alpha}PS2βPS. During the switch, stress fibres increase their length and change orientation, first changing by 90° and then reorienting back. The normal rapid reorientation requires new expression of {alpha}PS2βPS, which also permits recruitment of the adaptor protein tensin. Unexpectedly, it is the extracellular portion of the {alpha}PS2 subunit that provides the specificity for intracellular recruitment of tensin. Molecular variation of the integrin complex is thus a key component of developmentally programmed morphogenesis.

Key words: Integrin, Stress fibres, Follicle cells


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

Related articles in JCS:

Integrin swapping in focal adhesions

JCS 2009 122: 2305. [Full Text]  



This article has been cited by other articles:


Home page
 DevelopmentHome page
I. Delon and N. H. Brown
The integrin adhesion complex changes its composition and function during morphogenesis of an epithelium
Development, December 15, 2009; 136(24): e1 - e1.
[Full Text]


© The Company of Biologists Ltd 2009