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.
Conference Article| July 18 2013
ILK: a pseudokinase with a unique function in the integrin–actin linkage
Sara A. Wickström
Sara A. Wickström 1
1Paul Gerson Unna Group ‘Skin Homeostasis and Ageing’ Max Planck Institute for Biology of Ageing, Joseph-Stelzmann Strasse 9b, 50937 Cologne, Germany
1To whom correspondence should be addressed (firstname.lastname@example.org).
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Sushmita Ghatak, Jessica Morgner, Sara A. Wickström; ILK: a pseudokinase with a unique function in the integrin–actin linkage. Biochem Soc Trans 1 August 2013; 41 (4): 995–1001. doi: https://doi.org/10.1042/BST20130062
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