Phosphorylation of β3 integrin controls ligand binding strength

被引:64
作者
Datta, A [1 ]
Huber, F [1 ]
Boettiger, D [1 ]
机构
[1] Univ Penn, Dept Microbiol, Philadelphia, PA 19104 USA
关键词
D O I
10.1074/jbc.M109536200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The cytoplasmic domain of beta3 integrin contains tyrosines at positions 747 and 759 in domains that have been implicated in regulation of alpha(v)beta(3) function and that serve as potential substrates for Src family kinases. The phosphorylation level of beta(3) integrin was modulated using a temperature-sensitive v-Src kinase. Increased beta(3) phosphorylation abolished alpha(v)beta(3)- but not alpha(5)beta(1)-mediated adhesion to fibronectin. alpha(v)beta(3)-Mediated cell adhesion was restored by the expression of beta(3) containing Y747F or Y759F mutations but not by wild type beta(3) integrin. Thus, phosphorylation of the cytoplasmic domain of beta(3) is a negative regulator of alpha(v)beta(3)-fibronectin binding strength.
引用
收藏
页码:3943 / 3949
页数:7
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