ILK (integrin-linked kinase) is a central component of cell-matrix adhesions and an important regulator of integrin function. It forms a ternary complex with two other adaptor proteins, PINCH (particularly interesting cysteine- and histidine-rich protein) and parvin, forming the IPP (ILK-PINCH-parvin) complex that regulates the integrin-actin linkage as well as microtubule dynamics. These functions are essential for processes such as cell migration and matrix remodelling. The present review discusses the recent advances on the structural and functional characterization of ILK and the long-standing debate regarding its reported kinase activity.
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