Abstract

Cell-extracellular matrix (ECM) adhesion is crucial for control of cell behavior. It connects the ECM to the intracellular cytoskeleton and transduces bidirectional signals between the extracellular and intracellular compartments. The subcellular machinery that mediates cell-ECM adhesion and signaling is complex. It consists of transmembrane proteins (e.g., integrins) and at least several dozens of membrane-proximal proteins that assemble into a network through multiple protein interactions. Furthermore, despite sharing certain common components, cell-ECM adhesions exhibit considerable heterogeneity in different types of cells (e.g., the cell-ECM adhesions in cardiac myocytes are considerably different from those in fibroblasts). Here, we will first briefly describe the general properties of the integrin-mediated cell-ECM adhesion and signal transduction. Next, we will focus on one of the recently discovered cell-ECM adhesion protein complexes consisting of PINCH, integrin-linked kinase (ILK), and Parvin and use it as an example to illustrate the molecular basis underlying the assembly and functions of cell-ECM adhesions. Finally, we will discuss in detail the structure and regulation of cell-ECM adhesion complexes in cardiac myocytes, which illustrate the importance and complexity of the cell-ECM adhesion structures in organogenesis and diseases.