Adhesion sites, which interconnect cells with their neighbors or with the extracellular matrix (ECM), are large multiprotein complexes that provide mechanical coupling as well as a means for cells to sense the chemical and physical properties of their environment (Bershadsky et al., 2003; Chen et al., 2004; Geiger et al., 2001; Sastry and Burridge, 2000). The complex interplay between the mechanical role of cell adhesions and their ‘instructive role’, which is manifested by the activation of a wide variety of signaling networks, is mediated by a group of proteins collectively known as the

‘adhesome’. The concerted activity of adhesome components affects essentially all cellular functions, including morphogenesis, migration, proliferation, differentiation and viability (Berrier and Yamada, 2007; Streuli, 2009; Thiery, 2003; Vicente-Manzanares et al., 2009).

Adhesion to the ECM is mediated via heterodimeric transmembrane receptors, namely,-and-integrins. Combinations of among 18-chains and eight-chains form different heterodimers to yield a rich diversity of ECM receptors, enabling different cell types to respond differentially to variations in the ECM (Arnaout et al., 2005). On the cytoplasmic side of the adhesion sites, integrins can interact, via their cytoplasmic tails, with at least 12 different adaptor proteins (Zaidel-Bar et al., 2007a). Among these molecules, tensin (encoded by the TNS1 gene)(hereafter, the gene encoding each protein will be shown in italics in parentheses),