Focal adhesion kinase is not required for integrin function or viability in Drosophila
Focal adhesion kinase is not required for integrin function or viability in Drosophila
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DOI：
10.1242/dev.01462
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发表时间：
2004-12-01
期刊：
影响因子：
4.6
通讯作者：
Palmer, RH
中科院分区：
文献类型：
--
作者：
Grabbe, C;Zervas, CG;Palmer, RH
非受体蛋白酪氨酸激酶的哺乳动物粘着斑激酶（FAK）家族已经涉及控制对细胞表面整合素和G蛋白偶联受体的接合的多种细胞应答。哺乳动物蛋白质和果蝇FAK同源物Fak56之间的高水平序列保守性表明它具有相似的功能。然而，我们在这里表明，果蝇Fak56是不是必不可少的整合素功能的粘附，迁移或信号在体内。此外，缺乏Fak56的动物是可行的和可繁殖的，这表明Fak56对于其他发育或生理功能不是必需的。尽管如此，过表达的Fak56是整合素与细胞外基质结合的有效抑制剂，这表明Fak56可能在整合素粘附的负调节中发挥微妙的作用。
The mammalian focal adhesion kinase (FAK) family of non-receptor protein-tyrosine kinases has been implicated in controlling a multitude of cellular responses to the engagement of cell-surface integrins and G-protein-coupled receptors. The high level of sequence conservation between the mammalian proteins and the Drosophila homologue of FAK, Fak56, suggested that it would have similar functions. However, we show here that Drosophila Fak56 is not essential for integrin functions in adhesion, migration or signaling in vivo. Furthermore, animals lacking Fak56 are viable and fertile, demonstrating that Fak56 is not essential for other developmental or physiological functions. Despite this, overexpressed Fak56 is a potent inhibitor of integrins binding to the extracellular matrix, suggesting that Fak56 may play a subtle role in the negative regulation of integrin adhesion.