REGULATION OF FOCAL ADHESION-ASSOCIATED PROTEIN TYROSINE KINASE BY BOTH CELLULAR ADHESION AND ONCOGENIC TRANSFORMATION
REGULATION OF FOCAL ADHESION-ASSOCIATED PROTEIN TYROSINE KINASE BY BOTH CELLULAR ADHESION AND ONCOGENIC TRANSFORMATION
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DOI：
10.1038/358690a0
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发表时间：
1992-08-20
期刊：
影响因子：
64.8
通讯作者：
SHALLOWAY, D
中科院分区：
文献类型：
--
作者：
GUAN, JL;SHALLOWAY, D
越来越多的证据表明，细胞粘附受体的整合素家族可以将生化信号从细胞外基质传递到细胞内部，以调节细胞生长和分化1。我们已经表明，整合素/配体相互作用可以触发M（r）120，000（pp 120）蛋白的酪氨酸磷酸化，因此整合素的信号转导可能涉及细胞内蛋白酪氨酸激酶的激活，作为细胞与细胞外基质结合的早期事件2。在这里，我们报告说，pp 120是相同的局灶性粘附相关蛋白酪氨酸激酶pp 125 FAK（参考文献3，4）。我们发现，这种蛋白质的酪氨酸磷酸化是由细胞粘附和转化pp 60 v-src调制，这些磷酸化的变化与pp 125 FAK酪氨酸激酶活性增加。提出了一个模型，将这些发现与转化细胞的锚定非依赖性生长的分子基础。
INCREASING evidence indicates that the integrin family of cell adhesion receptors can transduce biochemical signals from the extracellular matrix to the cell interior to modulate cell growth and differentiation1. We have shown that integrin/ligand interactions can trigger tyrosine phosphorylation of a protein of M(r) 120,000 (pp120), so it is possible that signal transduction by integrins might involve activation of intracellular protein tyrosine kinases as an early event in cell binding to the extracellular matrix2. Here we report that pp120 is identical to the focal adhesion-associated protein tyrosine kinase pp125FAK (refs 3,4). We show that tyrosine phosphorylation of this protein is modulated both by cell adhesion and transformation by pp60v-src, and that these changes in phosphorylation are correlated with increased pp125FAK tyrosine kinase activity. A model is proposed to relate these findings to the molecular basis of anchorage-independent growth of transformed cells.