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The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase!

Sara A Wickström, Anika Lange, Eloi Montanez, Reinhard Fässler

Author Affiliations

  1. Sara A Wickström1,
  2. Anika Lange1,
  3. Eloi Montanez1 and
  4. Reinhard Fässler*,1
  1. 1 Department for Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried, Germany
  1. *Corresponding author. Department for Molecular Medicine, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried 82152, Germany. Tel.: +49 89 8578 2072; Fax: +49 89 8578 2422; E-mail: faessler{at}biochem.mpg.de
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Abstract

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.

  • Received October 19, 2009.
  • Accepted November 23, 2009.
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