Abbi S, Guan J L
Department of Molecular Medicine, Cornell University, Ithaca, NY 14853, USA.
Histol Histopathol. 2002 Oct;17(4):1163-71. doi: 10.14670/HH-17.1163.
Integrin-mediated cell adhesion to extracellular matrix (ECM) plays important roles in a variety of biological processes. Recent studies suggested that integrins mediate signal transduction across the plasma membrane via activating several intracellular signaling pathways. Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that has been shown to be a major mediator of integrin signal transduction pathways. Upon activation by integrins, FAK undergoes autophosphorylation as well as associations with several other intracellular signaling molecules. These interactions in the signaling pathways have been shown to regulation a variety of cellular functions such as cell spreading, migration, cell proliferation, apoptosis and cell survival. Recent progress in the understanding of FAK interactions with other proteins in the regulation of these cellular functions will be discussed in this review.
整合素介导的细胞与细胞外基质（ECM）的黏附在多种生物学过程中发挥着重要作用。最近的研究表明，整合素通过激活多种细胞内信号通路介导跨质膜的信号转导。黏着斑激酶（FAK）是一种非受体酪氨酸激酶，已被证明是整合素信号转导通路的主要介质。在被整合素激活后，FAK会发生自磷酸化，并与其他几种细胞内信号分子结合。这些信号通路中的相互作用已被证明可调节多种细胞功能，如细胞铺展、迁移、细胞增殖、凋亡和细胞存活。本文将讨论在理解FAK与其他蛋白质相互作用对这些细胞功能调节方面的最新进展。
