JCB logo
PeproTech: Free Shipping at www.peprotech.com
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 5 September 2006. doi:10.1083/jcb.200604060
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 6, 889-899
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 4954K)
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 Czuchra, A.
Right arrow Articles by Fässler, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Czuchra, A.
Right arrow Articles by Fässler, 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

Genetic analysis of ß1 integrin "activation motifs" in mice



Aleksandra Czuchra1, Hannelore Meyer1, Kyle R. Legate1, Cord Brakebusch2, and Reinhard Fässler1

1 Max Planck Institute of Biochemistry, Department of Molecular Medicine, 82152 Martinsried, Germany
2 University of Copenhagen, Department of Molecular Pathology, 2100 Copenhagen, Denmark

Correspondence to Reinhard Fässler: faessler{at}biochem.mpg.de

Akey feature of integrins is their ability to regulate the affinity for ligands, a process termed integrin activation. The final step in integrin activation is talin binding to the NPXY motif of the integrin ß cytoplasmic domains. Talin binding disrupts the salt bridge between the {alpha}/ß tails, leading to tail separation and integrin activation. We analyzed mice in which we mutated the tyrosines of the ß1 tail and the membrane-proximal aspartic acid required for the salt bridge. Tyrosine-to-alanine substitutions abolished ß1 integrin functions and led to a ß1 integrin–null phenotype in vivo. Surprisingly, neither the substitution of the tyrosines with phenylalanine nor the aspartic acid with alanine resulted in an obvious defect. These data suggest that the NPXY motifs of the ß1 integrin tail are essential for ß1 integrin function, whereas tyrosine phosphorylation and the membrane-proximal salt bridge between {alpha} and ß1 tails have no apparent function under physiological conditions in vivo.

Abbreviations used in this paper: Col1, collagen I; Erk, extracellular signal–regulated kinase; ES, embryonic stem; FA, focal adhesion; FN, fibronectin; HE, hematoxylin-eosin; K5, keratin 5; KI, knock-in; LN5, laminin 5; P, postnatal day.


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