FOCAL ADHESION PROTEIN-TYROSINE KINASE PHOSPHORYLATED IN RESPONSE TO CELL ATTACHMENT TO FIBRONECTIN
FOCAL ADHESION PROTEIN-TYROSINE KINASE PHOSPHORYLATED IN RESPONSE TO CELL ATTACHMENT TO FIBRONECTIN
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DOI：
10.1073/pnas.89.18.8487
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发表时间：
1992-09-15
影响因子：
11.1
通讯作者：
PATEL, SK
中科院分区：
文献类型：
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作者：
HANKS, SK;CALALB, MB;PATEL, SK
一个同源性为基础的cDNA克隆方法被用来确定一个广泛表达的蛋白酪氨酸激酶命名为“黏着斑激酶”（FadK）。整个小鼠FadK的氨基酸序列推导出的cDNA克隆，揭示了一个大的（119 kDa）非跨膜蛋白酪氨酸激酶，缺乏Src同源性SH 2和SH 3域。BALB/c 3 T3成纤维细胞的免疫染色显示FadK集中在局灶性粘连中。在BALB/c 3 T3细胞的生长培养物中，FadK在酪氨酸上磷酸化，但在通过胰蛋白酶消化分离的细胞中几乎不含或不含磷酸酪氨酸。当细胞重新铺在纤连蛋白上时，酪氨酸磷酸化状态在几分钟内恢复。FadK的激活可能是细胞与细胞外基质相互作用触发的细胞内信号转导途径中的重要早期步骤。
A homology-based cDNA cloning approach was used to identify a widely expressed protein-tyrosine kinase designated as "focal adhesion kinase" (FadK). The entire mouse FadK amino acid sequence was deduced from cDNA clones, revealing a large (119-kDa) non-membrane-spanning protein-tyrosine kinase that lacks Src-homology SH2 and SH3 domains. Immunostaining of BALB/c 3T3 fibroblasts revealed that FadK is concentrated in focal adhesions. FadK is phosphorylated on tyrosine in growing cultures of BALB/c 3T3 cells but contains little or no phosphotyrosine in cells detached by trypsinization. The tyrosine-phosphorylated state is regained within minutes when the cells are replated onto fibronectin. Activation of FadK may be an important early step in intracellular signal transduction pathways triggered in response to cell interactions with the extracellular matrix.