Integrins regulate the association and phosphorylation of paxillin by c-Abl
Integrins regulate the association and phosphorylation of paxillin by c-Abl
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DOI：
10.1074/jbc.273.23.14225
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发表时间：
1998-06-05
影响因子：
4.8
通讯作者：
Schwartz, MA
中科院分区：
文献类型：
--
作者：
Lewis, JM;Schwartz, MA
c-Abl原癌基因是一种非受体酪氨酸激酶，其活性和定位受整合素调节。细胞粘附到纤连蛋白触发c-Abl从细胞核到粘着斑的瞬时募集及其酪氨酸激酶的活化。为了研究c-Abl的整合素调节，测定了在细胞粘附后与c-Abl相互作用的蛋白质。几个蛋白质被磷酸化酪氨酸被发现瞬时共沉淀与c-Abl在细胞粘附过程中，和一个被确定为粘着斑蛋白桩蛋白。Abl也成为短暂的磷酸化响应细胞粘附。此外，桩蛋白被发现作为底物的粘附激活的c-Abl激酶。这些结果表明c-Abl可能通过磷酸化桩蛋白介导整合素对细胞功能的影响。
The c-Abl proto-oncogene is a non-receptor tyrosine kinase whose activity and localization are regulated by integrins. Cell adhesion to fibronectin triggers the transient recruitment of c-Abl from the nucleus to focal adhesions and activation of its tyrosine kinase. To investigate the integrin regulation of c-Abl, proteins that interact with c-Abl following cell adhesion were assayed. Several proteins that were phosphorylated on tyrosine were found to transiently co-precipitate with c-Abl during cell adhesion, and one was identified as the focal adhesion protein paxillin. Abl also became transiently phosphorylated in response to cell adhesion. In addition, paxillin was found to serve as substrate for the adhesion-activated c-Abl kinase. These results suggest that c-Abl may mediate effects of integrins on cell functions by phosphorylating paxillin.