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J. Biol. Chem., Vol. 277, Issue 6, 3943-3949, February 8, 2002
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From the Department of Microbiology, University of Pennsylvania,
Philadelphia, Pennsylvania 19104-6076
The cytoplasmic domain of
Phosphorylation of
3 Integrin Controls Ligand
Binding Strength*
3
integrin contains tyrosines at positions 747 and 759 in domains that
have been implicated in regulation of 
v3
function and that 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 wild type 3 integrin. Thus, phosphorylation
of the cytoplasmic domain of 3 is a negative regulator
of v3-fibronectin binding strength.
*
This research was supported National Institutes of Health
Grants CA16502 and GM57388.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Microbiology, University of Pennsylvania, Philadelphia, PA 19104-6076. Tel.: 215-898-8792; Fax: 215-898-9557. E-mail:
boettige@mail.med.upenn.edu.
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