Integrin-linked protein kinase (ILK) (ILK)

Integrin-linked protein kinase (ILK) is a multifunctional protein that serves as a critical hub in the focal adhesion complex, linking the cytoplasmic tails of beta-integrins to the actin cytoskeleton (UniProt: Q13418). It functions primarily as a scaffold within the heterotrimeric IPP complex, comprising ILK, PINCH, and Parvin, which is essential for regulating cell shape, motility, and survival signaling pathways (PubMed: 25633450). Although its classification as an active kinase is debated due to the absence of certain conserved catalytic residues, ILK is known to modulate key signaling pathways, including the phosphorylation of AKT and the regulation of GSK3-beta (PubMed: 16113678). In pathological contexts, ILK is frequently overexpressed, driving oncogenic processes such as epithelial-mesenchymal transition (EMT), metastasis, and resistance to apoptosis in various cancers (PubMed: 29730545). Additionally, ILK plays a significant role in the progression of chronic kidney disease and pulmonary fibrosis by promoting myofibroblast activation (PubMed: 22451718). Therapeutic strategies targeting ILK include small molecule inhibitors like QLT0267, which aim to disrupt its signaling and scaffolding functions to treat malignancy and fibrotic disorders (PubMed: 16432178).

Other names

ILK1ILK2P59p59ILKIntegrin-linked kinase

Inhibition of the ATP-binding site to disrupt kinase-like signaling and destabilization of the ILK-PINCH-Parvin (IPP) complex to impair focal adhesion assembly and downstream AKT/GSK3-beta signaling (PubMed: 16432178, PubMed: 25633450).