AUTONOMOUS EXPRESSION OF A NONCATALYTIC DOMAIN OF THE FOCAL ADHESION-ASSOCIATED PROTEIN TYROSINE KINASE PP125FAK
AUTONOMOUS EXPRESSION OF A NONCATALYTIC DOMAIN OF THE FOCAL ADHESION-ASSOCIATED PROTEIN TYROSINE KINASE PP125FAK
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DOI：
10.1128/mcb.13.2.785
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发表时间：
1993-02-01
影响因子：
5.3
通讯作者：
PARSONS, JT
中科院分区：
文献类型：
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作者：
SCHALLER, MD;BORGMAN, CA;PARSONS, JT
整合素在细胞粘附和细胞骨架锚定中发挥核心作用，并参与细胞内信号的产生，包括酪氨酸磷酸化。我们最近分离出一种 cDNA，编码一种独特的粘着斑相关蛋白酪氨酸激酶 (FAK)，它是整合素介导的信号转导途径的一个组成部分。在这里，我们报告了编码 FAK 激酶 C 端非催化结构域的 cDNA 的分离，称为 FRNK（FAK 相关非激酶）。 FAK 和 FRNK 编码的多肽 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，表明 pp125FAK 通过其 C 端结构域内的序列定向至粘着斑。我们还表明，pp125FAK 酪氨酸磷酸化的纤连蛋白依赖性增加伴随着 p41FRNK 的翻译后修饰。
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.