Matrix Dynamics Group, University of Toronto, Toronto, Ontario, Canada.
FEBS Lett. 2011 Jan 3;585(1):18-22. doi: 10.1016/j.febslet.2010.11.033. Epub 2010 Nov 21.
Cell adhesion, spreading and migration on extracellular matrices are regulated by complex processes that involve the cytoskeleton and a large array of adhesion receptors, including the β1 integrin. Filamin A is a large, multi-domain, homodimeric actin binding protein that contributes to the mechanical stability of cells and interacts with several proteins that regulate cell adhesion including β1 integrin and several protein kinases. Here we review current data on the structure, mechanical properties and intracellular signaling functions of filamin that regulate cell adhesion. We also consider new data showing that interactions of filamin A with intermediate filaments and protein kinase C enable tight regulation of β1 integrin function and consequently early events in cell adhesion and migration on extracellular matrix proteins.
细胞在细胞外基质上的黏附、铺展和迁移受到复杂过程的调控,其中涉及细胞骨架和大量黏附受体,包括β1 整合素。细丝蛋白 A 是一种大型的、多结构域的同二聚体肌动蛋白结合蛋白,它有助于细胞的机械稳定性,并与几种调节细胞黏附的蛋白质相互作用,包括β1 整合素和几种蛋白激酶。在这里,我们综述了细丝蛋白 A 的结构、力学特性和细胞内信号转导功能的最新数据,这些功能调节细胞黏附。我们还考虑了新的数据,表明细丝蛋白 A 与中间丝和蛋白激酶 C 的相互作用能够紧密调节β1 整合素的功能,从而调节细胞在细胞外基质蛋白上的黏附和迁移的早期事件。