Focal adhesions (FAs) are specialized, transmembrane complexes that mediate integrin-dependent adhesion between cells and the extracellular matrix (ECM). The submembrane plaque at these sites contains more than 50 known proteins that link the actin cytoskeleton to the membrane. In Cell Science at a Glance on page 3577, Eli Zamir and Benny Geiger provide a FA ‘wiring diagram’, showing the known components and their reported interactions. Then, in a Commentary on page 3583, Zamir and Geiger discuss the complexity, diversity and dynamics of FAs in more detail. The complexity of FAs is further extended by post-translational modifications, proteolytic processing and alternative splicing of many of their components. Furthermore, the latter can potentially assemble in numerous ways to generate distinct supramolecular assemblies, such as fibrillar adhesions and focal complexes. These structures are by no means static: activation of Rho causes focal complexes to mature into ‘classical’ FAs, and studies using...
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In this issue. J Cell Sci 15 October 2001; 114 (20): e20. doi:
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