REGULATION OF ADHESION, SIGNALING AND ANGIOGENESIS BY

Cancer development requires the acquisition of several capabilities that include enhanced replicative potential, anchorage and growth factor independence, evasion of apoptosis, angiogenesis and tumour invasion and metastasis. One protein that has emerged as promoting many of these phenotypes when dysregulated is Integrin-Linked Kinase (ILK), a unique intracellular adaptor and kinase that links the cell adhesion receptors, integrins, and growth factors to the actin cytoskeleton and to a variety of signalling pathways. The recent findings of elevated levels of ILK in various cancers, and that inhibition of ILK expression and activity is anti-tumourigenic, makes ILK an attractive target for cancer therapeutics. ILK was identified as an integrin β-subunit cytoplasmic domain interactor1. Since then, genetic studies in model organisms such as Drosophilla melanogaster2, Caenorhabditis elegans3 and mice4, and cell biological studies in cultured cells, have established an important and essential role of ILK in connecting integrins to the actin cytoskeleton, and in regulating actin polymerization5. Proteins such a