Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase.
Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase.
复制标题
DOI：
10.1016/s0021-9258(18)35853-8
复制
发表时间：
1992-11
期刊：
影响因子：
--
通讯作者：
L. Kornberg;H. Earp;J. Parsons;M. D. Schaller;Rudy L. Juliano
中科院分区：
文献类型：
--
作者：
L. Kornberg;H. Earp;J. Parsons;M. D. Schaller;Rudy L. Juliano
我们最近已经表明，130-kDa蛋白（pp130）的酪氨酸磷酸化的变化可能涉及整联蛋白信号传导（Kornberg，L.，厄普，H.S.，特纳角，Prokop和Juliano，R. L.等人（1991）Proc. Acad. sci. U.S.A.88，8392 - 8396）。pp130蛋白质复合物的一种组分与针对p125fak产生的抗体反应，p125fak是一种局灶性接触相关酪氨酸激酶（Schlier，M.D.，博格曼角一、CobB，B.美国，瓦因斯河R.，雷诺兹，A. B.，和Parsons，J.T.等人（1992）Proc. Acad. sci.美国89，5192 - 5196）。抗体介导的整合素聚集和KB细胞与纤连蛋白的粘附均导致p125fak的酪氨酸磷酸化增加。p125fak的磷酸化与细胞对纤连蛋白的粘附一致，并且在细胞铺展之前达到最大。当KB细胞粘附于纤连蛋白、IV型胶原或层粘连蛋白时，p125 fak的酪氨酸磷酸化被诱导，但在多聚赖氨酸上不被诱导。当KB细胞进行间接免疫荧光显微镜，p125fak共定位与塔林在焦点接触。这些数据提供了酪氨酸激酶参与整合素信号传导的额外证据。
We have recently shown that changes in tyrosine phosphorylation of a 130-kDa protein(s) (pp130) may be involved in integrin signaling (Kornberg, L., Earp, H.S., Turner, C., Prokop, and Juliano, R. L. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 8392-8396). One component of the pp130 protein complex reacts with an antibody generated against p125fak, which is a focal contact-associated tyrosine kinase (Schaller, M.D., Borgman, C. A., Cobb, B. S., Vines, R. R., Reynolds, A. B., and Parsons, J. T. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 5192-5196). Both antibody-mediated integrin clustering and adhesion of KB cells to fibronectin leads to increased tyrosine phosphorylation of p125fak. The phosphorylation of p125fak is coincident with adhesion of cells to fibronectin and is maximal prior to cell spreading. Tyrosine phosphorylation of p125fak is induced when KB cells are allowed to adhere to fibronectin, collagen type IV, or laminin, but is not induced on polylysine. When KB cells are subjected to indirect immunofluorescence microscopy, p125fak colocalizes with talin in focal contacts. These data provide additional evidence that tyrosine kinases are involved in integrin signaling.