Department for Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried, Germany.
EMBO J. 2010 Jan 20;29(2):281-91. doi: 10.1038/emboj.2009.376. Epub 2009 Dec 24.
Dynamic interactions of cells with their environment regulate multiple aspects of tissue morphogenesis and function. Integrins are the major class of cell surface receptors that recognize and bind extracellular matrix proteins, resulting in the engagement and organization of the cytoskeleton as well as activation of signalling pathways to regulate cell behaviour and morphogenetic processes. The ternary complex of integrin-linked kinase (ILK), PINCH, and parvin (IPP complex), which was identified more than a decade ago, interacts with the cytoplasmic tail of beta integrins and couples them to the actin cytoskeleton. In addition, ILK has been shown to act as a serine/threonine kinase and to directly activate several signalling pathways downstream of integrins. However, the kinase activity of ILK and the precise functions of the IPP complex have remained elusive and controversial. This review focuses on the recent advances made towards understanding the specialized roles this complex and its individual components have acquired during evolution.
细胞与环境的动态相互作用调节组织形态发生和功能的多个方面。整合素是细胞表面受体的主要类别，可识别和结合细胞外基质蛋白，导致细胞骨架的结合和组织以及信号通路的激活，从而调节细胞行为和形态发生过程。十多年前发现的整合素连接激酶 (ILK)、PINCH 和 parvin (IPP 复合物) 的三元复合物与β整合素的细胞质尾巴相互作用，并将其与肌动蛋白细胞骨架偶联。此外，ILK 已被证明作为丝氨酸/苏氨酸激酶发挥作用，并直接激活整合素下游的几个信号通路。然而，ILK 的激酶活性和 IPP 复合物的确切功能仍然难以捉摸且存在争议。这篇综述重点介绍了在理解该复合物及其各个成分在进化过程中获得的专门作用方面取得的最新进展。
