The PINCH-ILK-parvin complex (Tu et al., 2001; Zhang et al., 2002; Li et al., 1999) localizes to focal adhesions and plays a critical role in the regulation of cell adhesion, cell shape modulation, motility and ECM deposition (Velyvis et al., 2001; Braun et al, 2003). ILK binds PINCH through its N-terminal domain and binds PARVA or PARVB through its C-terminal domain, resulting in formation of the ternary PINCH-ILK-parvin complex (Tu et al., 2001). These complexes form before they are localized to integrin-rich adhesion sites (Zhang et al., 2002). Formation of the ILK-PINCH-parvin complexes stabilizes these proteins by protecting them from degradation by the proteasome (Fukuda et al., 2003).