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Papers In Press, published online ahead of print November 26, 2001
Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104
Corresponding Author: boettige{at}mail.med.upenn.edu
The cytoplasmic domain of
J. Biol. Chem, 10.1074/jbc.M109536200
Submitted on October 2, 2001
Revised on November 19, 2001
Accepted on November 25, 2001
Phosphorylation of beta3 integrin controls ligand binding strength
3 integrin contains tyrosines at positions 747 and 759 in domains which have been implicated in regulation of 
v3 function and which serve as potential substrates for src family kinases. The phosphorylation level of 3 integrin was modulated using a temperature-sensitive v-src kinase. Increased 3 phosphorylation abolished v3- but not 51-mediated adhesion to fibronectin. v3-mediated cell adhesion was restored by the expression of 3 containing Y747F or Y759F mutations but not by wt 3 integrin. Thus, phosphorylation of the cytoplasmic domain of 3 is a negative regulator of v3-fibronectin binding strength.
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