Dedhar S, Williams B, Hannigan G
BC Cancer Agency and Dept of Biochemistry and Molecular Biology, University of BC, Jack Bell Research Centre, 2660 Oak Street, Vancouver, B.C., Canada V6H 3ZH.
Trends Cell Biol. 1999 Aug;9(8):319-23. doi: 10.1016/s0962-8924(99)01612-8.
Interaction of cells with the extracellular matrix (ECM) results in the regulation of cell growth, differentiation and migration by coordinated signal transduction through integrins and growth-factor receptors. Integrins achieve signalling by interacting with intracellular effectors that couple integrins and growth-factor receptors to downstream components. One well-studied effector is focal-adhesion kinase (FAK), but recently another protein kinase, integrin-linked kinase (ILK), has been identified as a receptor-proximal effector of integrin and growth-factor signalling. ILK appears to interact with and be influenced by a number of different signalling pathways, and this provides new routes for integrin-mediated signalling. This article discusses ILK structure and function and recent genetic and biochemical evidence about the role of ILK in signal transduction.
细胞与细胞外基质(ECM)的相互作用通过整合素和生长因子受体的协同信号转导来调节细胞生长、分化和迁移。整合素通过与细胞内效应器相互作用来实现信号传导,这些效应器将整合素和生长因子受体与下游成分连接起来。一种研究充分的效应器是粘着斑激酶(FAK),但最近另一种蛋白激酶,即整合素连接激酶(ILK),已被确定为整合素和生长因子信号传导的受体近端效应器。ILK似乎与许多不同的信号通路相互作用并受其影响,这为整合素介导的信号传导提供了新途径。本文讨论了ILK的结构和功能以及关于ILK在信号转导中作用的最新遗传学和生物化学证据。