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神经肽和生长因子作用中的酪氨酸磷酸化。

Tyrosine phosphorylation in the action of neuropeptides and growth factors.

作者信息

Rozengurt E, Rodríguez-Fernández J L

机构信息

Growth Regulation Laboratory, Imperial Cancer Research Fund, London, U.K.

出版信息

Essays Biochem. 1997;32:73-86.

PMID:9493012
Abstract

The non-receptor tyrosine kinase p125FAK and the adaptor proteins paxillin and p130CAS are implicated in signal transduction at the focal adhesion plaques. An increase in the tyrosine phosphorylation of p125FAK, paxillin and p130CAS has been identified as an early signal in response to integrin engagement, mitogenic neuropeptides, bioactive lipids and growth factors. Agonist-mediated induction of tyrosine phosphorylation of focal adhesion proteins occurs through a PKC and Ca(2+)-independent pathway that is critically dependent on the integrity of the actin cytoskeleton and on functional Rho. The coordinate tyrosine phosphorylation of p125FAK, paxillin and p130CAS plays a role in cell locomotion, DNA synthesis and apoptosis.

摘要

非受体酪氨酸激酶p125FAK以及衔接蛋白桩蛋白和p130CAS参与粘着斑处的信号转导。p125FAK、桩蛋白和p130CAS的酪氨酸磷酸化增加已被确定为对整合素结合、促有丝分裂神经肽、生物活性脂质和生长因子作出反应的早期信号。激动剂介导的粘着斑蛋白酪氨酸磷酸化的诱导通过一条不依赖蛋白激酶C(PKC)和钙离子(Ca2+)的途径发生,该途径严重依赖于肌动蛋白细胞骨架的完整性和功能性Rho。p125FAK、桩蛋白和p130CAS的协同酪氨酸磷酸化在细胞运动、DNA合成和细胞凋亡中发挥作用。

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