Focal adhesion kinase tyrosine phosphorylation is associated with myogenesis and modulated by insulin
Focal adhesion kinase tyrosine phosphorylation is associated with myogenesis and modulated by insulin
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DOI：
10.1046/j.1365-2184.2002.00232.x
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发表时间：
2002-06-01
影响因子：
8.5
通讯作者：
Dey, CS
中科院分区：
文献类型：
--
作者：
Goel, HL;Dey, CS
作为 C2Cl2 小鼠骨骼肌细胞分化的功能，粘着斑激酶 (FAK) 被严重磷酸化。在增殖细胞稳定之前，胰岛素引起 FAK 磷酸化增加，而在分化细胞中，刺激前 FAK 磷酸化会出现一致的短暂抑制。 FAK的表达水平没有改变。胰岛素受体酪氨酸激酶活性的特异性抑制消除了胰岛素介导的 FAK 去磷酸化。数据强烈表明，骨骼肌分化所必需的 FAK 酪氨酸磷酸化受到胰岛素的调节。因此，我们首次报道了骨骼肌分化过程中胰岛素对 FAK 酪氨酸磷酸化的差异调节。
Focal adhesion kinase (FAK) was heavily phosphorylated as a function of differentiation of C2Cl2 mouse skeletal muscle cells. Insulin caused increases in FAK phosphorylation before stabilization in proliferated cells, while in differentiated cells there was a consistent transient inhibition of FAK phosphorylation before stimulation. The expression level of FAK was unaltered. Specific inhibition of insulin receptor tyrosine kinase activity abolished the insulin-mediated dephosphorylation of FAK. The data strongly indicate that FAK tyrosine phosphorylation, necessary for skeletal muscle differentiation, is modulated by insulin. Thus, for the first time, we report the differential regulation of FAK tyrosine phosphorylation by insulin during skeletal muscle differentiation.