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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
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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.


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