Abstract

Integrin-linked kinase (ILK) is a recently identified cytoplasmic protein serine/threonine kinase implicated in integrin-, growth factor- and Wnt-signaling pathways. It contains several structurally conserved motifs including ankyrin repeats, pleckstrin-homology (PH) domain and protein kinase catalytic domain that are critical for signal transduction. Recent studies have documented that ILK plays important roles in bi-directional ( and ) transmembrane signaling pathways via integrins and other proteins, leading to regulation of cell adhesion, growth, survival, extracellular matrix deposition and potentially differentiation. Furthermore, ILK is implicated in tumorigenesis and ILK appears to be a useful diagnostic marker of certain human tumors. The identification of novel ILK-associated proteins will provide a better understanding of how ILK functions in intracellular signal transduction cascades and tumorigenesis.

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