Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA.
Curr Opin Cell Biol. 2012 Oct;24(5):607-13. doi: 10.1016/j.ceb.2012.06.003. Epub 2012 Jul 2.
Integrin-linked kinase (ILK) is a widely expressed and evolutionally conserved component of cell-extracellular matrix (ECM) adhesions. Although initially named as a kinase, ILK contains an unusual pseudoactive site that is incapable of catalyzing phosphorylation. Instead, ILK acts as a central component of a heterotrimer (the PINCH-ILK-parvin complex) at ECM adhesions mediating interactions with a large number of proteins via multiple sites including its pseudoactive site. Through higher level protein-protein interactions, this scaffold links integrins to the actin cytoskeleton and catalytic proteins and thereby regulates focal adhesion assembly, cytoskeleton organization and signaling. This review summarizes recent advances in our understanding of the structure and functions of the PINCH-ILK-parvin complex, and discusses emerging new features of the molecular mechanisms by which it regulates diverse cellular, physiological and pathological processes.
整合素连接激酶（ILK）是细胞-细胞外基质（ECM）黏附中广泛表达和进化上保守的成分。虽然最初被命名为激酶，但 ILK 含有一个不寻常的伪活性位点，不能催化磷酸化。相反，ILK 作为 ECM 黏附中异三聚体（PINCH-ILK-Parvin 复合物）的一个核心组成部分，通过多个位点（包括其伪活性位点）与大量蛋白质相互作用。通过更高水平的蛋白质-蛋白质相互作用，这个支架将整合素与肌动蛋白细胞骨架和催化蛋白连接起来，从而调节焦点黏附的组装、细胞骨架的组织和信号转导。这篇综述总结了我们对 PINCH-ILK-Parvin 复合物结构和功能的最新认识，并讨论了其调节多种细胞、生理和病理过程的分子机制的新出现的特征。
