Adhesion plaques: sites of transmembrane interaction between the extracellular matrix and the actin cytoskeleton

Abstract

In this paper we review what is known about the organization of adhesion plaques, the regions where cells in culture adhere most tightly to the underlying substratum. These specialized areas of the plasma membrane serve as attachment sites for stress fibres. A major objective has been to determine how microfilament bundles are anchored at such regions. In their morphology and composition adhesion plaques resemble the adhesions fibroblasts make to the extracellular matrix. Some extracellular matrix components have been identified on the outside face of adhesion plaques. Within the plasma membrane of adhesion plaques, extracellular matrix receptors, such as the fibronectin receptor (integrin), have been identified. This transmembrane glycoprotein complex has been shown to bind the cytoplasmic protein talin, which, in turn, associates with vinculin. These proteins establish a transmembrane chain of attachment between the extracellular matrix and the cytoskeleton, although how the actin filaments interact with these components remains to be determined. Besides having a structural function, adhesion plaques may also be regions where regulatory signals are transmitted across the membrane. Consistent with this idea has been the finding that various tyrosine kinases and a calcium-dependent protease are concentrated at the cytoplasmic aspect of adhesion plaques. Furthermore, several adhesion plaque proteins become phosphorylated during cell transformation by Rous sarcoma virus. In future work it will be important to determine how such modifications affect the interactions of these proteins and the stability of adhesion plaques.