Tensin contains three actin-binding domains (ABDs) that allows it to form crosslinks along actin filaments; it also prevents actin assembly by capping actin filaments at the barbed end [5, 6]. Tensin has numerous phosphorylation sites and multiple protein interaction domains for both structural components (e.g. paxillin, β-integrin [7]) and signaling molecules (e.g. Src, phosphatidylinositol 3-kinase [PI3K], focal adhesion kinase [FAK]) [8] (reviewed in [2]). Phosphorlyation of tensin corresponds with cell-ECM binding [9] and growth factor stimulation [10] (reviewed in [1]). Tensin forms a C-shaped structure [11] that binds focal adhesion components at both ends [12]. Tensin is also proposed to form a dimer via its carboxy-terminus and this association may be dependent upon its phosphorylation state [11].

Protein localization and function

Tensin primarily localizes to sites of cell attachment such as focal adhesions [12, 13], elongated fibrillar structures (aka fibrillar adhesions)[14] and possibly other adhesive junctions [15]. Tensin serves as a link between signal transduction pathways and the actin cytoskeleton by forming a structural platform that regulates the assembly of focal adhesion components, phosphoproteins, and signaling molecules for processes such as cell migration [12, 16] and tissue regeneration [17].