Schaller M D, Borgman C A, Parsons J T
Department of Microbiology and Cancer Center, University of Virginia Health Sciences Center, Charlottesville 22908.
Mol Cell Biol. 1993 Feb;13(2):785-91. doi: 10.1128/mcb.13.2.785-791.1993.
Integrins play a central role in cellular adhesion and anchorage of the cytoskeleton and participate in the generation of intracellular signals, including tyrosine phosphorylation. We have recently isolated a cDNA encoding a unique, focal adhesion-associated protein tyrosine kinase (FAK) that is a component of an integrin-mediated signal transduction pathway. Here we report the isolation of cDNAs encoding the C-terminal, noncatalytic domain of the FAK kinase, termed FRNK (FAK-related nonkinase). Both the FAK- and FRNK-encoded polypeptides, pp125FAK and p41/p43FRNK, are expressed in normal chicken embryo cells. pp125FAK and p41/p43FRNK were localized to focal adhesions, suggesting that pp125FAK is directed to the focal adhesions by sequences within its C-terminal domain. We also show that the fibronectin-dependent increase in tyrosine phosphorylation of pp125FAK is accompanied by a concomitant posttranslational modification of p41FRNK.
整合素在细胞黏附以及细胞骨架的锚定中发挥核心作用，并参与包括酪氨酸磷酸化在内的细胞内信号的产生。我们最近分离出了一个编码独特的、与粘着斑相关的蛋白酪氨酸激酶（FAK）的cDNA，该激酶是整合素介导的信号转导途径的一个组成部分。在此，我们报告编码FAK激酶C末端非催化结构域（称为FRNK，即FAK相关非激酶）的cDNA的分离。FAK和FRNK编码的多肽，即pp125FAK和p41/p43FRNK，均在正常鸡胚细胞中表达。pp125FAK和p41/p43FRNK定位于粘着斑，这表明pp125FAK是通过其C末端结构域内的序列被导向粘着斑的。我们还表明，纤连蛋白依赖的pp125FAK酪氨酸磷酸化增加伴随着p41FRNK的翻译后修饰。
