The parvins

The actin cytoskeleton plays a critical role in maintaining cellular shape, regulating cell motility and responding to mechanical strain. It is highly dynamic and responds to extracellular stimuli, such as hormones and growth factors, cell-cell adhesion and variations in the extracellular matrix (ECM). Cell-ECM adhesion is mediated primarily by integrins and associated proteins. Integrins function as transmembrane receptors for ECM proteins such as fibronectin, laminin and collagen. Through protein complexes associated with their cytoplasmic domain, such as those containing talin, integrin-linked kinase (ILK), PINCH, parvin, paxillin and/or focal adhesion kinase (FAK), integrins transduce bi-directional signals between the ECM and intracellular signaling pathways. Integrin-associated proteins can integrate cell adhesion-mediated signaling with other extracellular signals, such as those originating from growth factor receptors, through a variety of intracellular signaling pathways. In addition to regulating cell survival, proliferation and gene expression, integrin-mediated signaling often results in changes in the actin cytoskeleton leading to cell shape change and motility. In this article, we will review current knowledge about a family of proteins, the parvins, which play a critical role in transducing signals from integrins to the actin cytoskeleton and intracellular signaling proteins.