Tensin is involved in the maintenance of cellular structure by anchoring Actin filaments at the focal adhesion via F-Actin binding and capping activities. However, tensin also contains a Src homology 2 (SH2) domain and has the ability to be phosphorylated. Tensin is phosphorylated on tyrosine, serine, and threonine residues, suggesting that it might participate in signal transduction cascades. These diverse characteristics in a single molecule indicate that tensin may be an important link between the cytoskeleton and signal transduction pathways.