Transduction of extracellular matrix signals through integrins influences intracellular and extracellular functions, and appears to require interaction of integrin cytoplasmic domains with cellular proteins. Integrin-linked kinase (ILK) is an ankyrin repeat containing 51 kDa receptor-proximate serine-threonine kinase (1), with a reported migration rate of 59K. This 451 amino acid protein interacts with the cytoplasmic domain of the beta-1 integrin subunit and contains sequence motifs found in pleckstrin homology domains capable of interacting with phosphoinositide lipids. ILK is an upstream regulator of Pi(3)K dependant activation of protein kinase B (PKB/AKT) and inhibition of glycogen synthase kinase 3 (GSK-3). ILK2 expression is associated with mediation of cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. ILK2 is overexpressed in some highly invasive tumor cell lines.

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