EMBO Member's Review
The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase!
Article first published online: 24 DEC 2009
Copyright © 2010 European Molecular Biology Organization
The EMBO Journal
Volume 29, Issue 2, pages 281–291, January 20, 2010
How to Cite
Wickström, S. A., Lange, A., Montanez, E. and Fässler, R. (2010), The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase!. The EMBO Journal, 29: 281–291. doi: 10.1038/emboj.2009.376
- Issue published online: 20 JAN 2010
- Article first published online: 24 DEC 2009
- Manuscript Accepted: 23 NOV 2009
- Manuscript Received: 19 OCT 2009
- integrin-linked kinase;
- tissue morphogenesis
Dynamic interactions of cells with their environment regulate multiple aspects of tissue morphogenesis and function. Integrins are the major class of cell surface receptors that recognize and bind extracellular matrix proteins, resulting in the engagement and organization of the cytoskeleton as well as activation of signalling pathways to regulate cell behaviour and morphogenetic processes. The ternary complex of integrin-linked kinase (ILK), PINCH, and parvin (IPP complex), which was identified more than a decade ago, interacts with the cytoplasmic tail of β integrins and couples them to the actin cytoskeleton. In addition, ILK has been shown to act as a serine/threonine kinase and to directly activate several signalling pathways downstream of integrins. However, the kinase activity of ILK and the precise functions of the IPP complex have remained elusive and controversial. This review focuses on the recent advances made towards understanding the specialized roles this complex and its individual components have acquired during evolution.