A point mutation of integrin beta 1 subunit blocks binding of alpha 5 beta 1 to fibronectin and invasin but not recruitment to adhesion plaques.
A point mutation of integrin beta 1 subunit blocks binding of alpha 5 beta 1 to fibronectin and invasin but not recruitment to adhesion plaques.
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DOI：
10.1083/jcb.119.4.913
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发表时间：
1992-11
影响因子：
7.8
通讯作者：
Ginsberg, M H
中科院分区：
文献类型：
--
作者：
Takada, Y;Ylanne, J;Mandelman, D;Puzon, W;Ginsberg, M H
β 1亚基高度保守区域中的点突变，Asp 130替换为Ala（D130 A），消除了α 5 β 1与纤连蛋白（FN）的Arg-Gly-Asp（RGD）依赖性结合，而不破坏总体结构或异源二聚体组装。D130 A突变还干扰与侵袭素（一种缺乏RGD序列的配体）的结合。尽管α 5 β 1（D130 A）无法检测到FN结合，但内源性仓鼠受体可将其募集至FN上形成的粘附斑。因此，完整的配体结合功能对于将α 5 β 1募集至粘附斑是不需要的。β 1（D130 A）的过表达部分干扰内源性α 5 β 1功能，从而定义显性负性β 1整合素突变。
A point mutation in a highly conserved region of the beta 1 subunit, Asp130 to Ala (D130A) substitution, abrogates the Arg-Gly-Asp (RGD)- dependent binding of alpha 5 beta 1 to fibronectin (FN) without disrupting gross structure or heterodimer assembly. The D130A mutation also interferes with binding to invasin, a ligand that lacks RGD sequence. In spite of the lack of detectable FN binding by alpha 5 beta 1(D130A), it was recruited to adhesion plaques formed on FN by endogenous hamster receptors. Thus, intact ligand binding function is not required for recruitment of alpha 5 beta 1 to adhesion plaques. Overexpression of beta 1(D130A) partially interfered with endogenous alpha 5 beta 1 function, thus defining a dominant negative beta 1 integrin mutation.