“…The globular talin head contains a FERM (four-point-one, ezrin, radixin, moesin) domain (residues 86-400) with binding sites for β-integrin cytodomains [6], and two signalling proteins, FAK (focal adhesion kinase) [7] and the type 1γ 661 isoform of PIPK (phosphatidylinositol-4-phosphate 5-kinase) [8,9], which regulate the dynamic properties of integrin-containing cell-extracellular matrix junctions or FAs (focal adhesions). The FERM domain also contains an actin-binding site [10], and there is an adjacent membrane insertion sequence [11] which may account for the ability of talin to create holes in liposomes [12,13]. The talin rod, which is responsible for dimer formation, contains a conserved C-terminal actin-binding site [14,15] homologous to that in Hip1R (Huntingtin-interacting protein 1-related) and yeast Sla2p [16], a second integrin-binding site [17,18], and several binding sites for the cytoskeletal protein vinculin [19,20], which itself has multiple binding partners, including F-actin [21].…”