ILK

Description

The ILK (integrin linked kinase) is a protein-coding gene located on chromosome 11.

Integrin-linked kinase is an enzyme that in humans is encoded by the ILK gene involved with integrin-mediated signal transduction. Mutations in ILK are associated with cardiomyopathies. It is a 59kDa protein originally identified in a yeast-two hybrid screen with integrin β1 as the bait protein. Since its discovery, ILK has been associated with multiple cellular functions including cell migration, proliferation, and adhesion. Integrin-linked kinases (ILKs) are a subfamily of Raf-like kinases (RAF). The structure of ILK consists of three features: 5 ankyrin repeats in the N-terminus, Phosphoinositide binding motif and extreme N-terminus of kinase catalytic domain. Integrins lack enzymatic activity and depend on adapters to signal proteins. ILK is linked to beta-1 and beta-3 integrin cytoplasmic domains and is one of the best described integrins. Although first described as a serine/threonine kinase by Hannigan, important motifs of ILK kinases are still uncharacterized. ILK is thought to have a role in development regulation and tissue homeostasis, however it was found that in flies, worms and mice ILK activity isn't required to regulate these processes.

ILK is a receptor-proximal protein kinase that regulates integrin-mediated signal transduction. It may act as a mediator of inside-out integrin signaling and is a focal adhesion protein that is part of the ILK-PINCH complex. This complex is a convergence point for integrin and growth factor signaling pathways. ILK may be involved in mediating cell architecture, adhesion to integrin substrates, and anchorage-dependent growth in epithelial cells. It regulates cell motility by forming a complex with PARVB. ILK phosphorylates beta-1 and beta-3 integrin subunits on serine and threonine residues, as well as AKT1 and GSK3B.

ILK is also known as HEL-S-28, ILK-1, ILK-2, P59, p59ILK.

Associated Diseases

WES Whole Exome Sequencing

Clinical Exome Sequencing