Integrin-linked kinase
Protein-coding gene in the species Homo sapiens / From Wikipedia, the free encyclopedia
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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.[5][6] It is a 59kDa protein originally identified in a yeast-two hybrid screen with integrin β1 as the bait protein.[7] 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.[8] Integrins lack enzymatic activity and depend on adapters to signal proteins.[8] ILK is linked to beta-1 and beta-3 integrin cytoplasmic domains and is one of the best described integrins.[9] Although first described as a serine/threonine kinase by Hannigan,[7] important motifs of ILK kinases are still uncharacterized.[9] 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.[9]
Animal ILKs have been linked to the pinch- parvin complex which control muscle development.[9] Mice lacking ILK were embryonic lethal due to lack of organized muscle cell development.[9] In mammals ILK lacks catalytic activity but supports scaffolding protein functions for focal adhesions.[9] In plants, ILKs signal complexes to focal adhesion sites.[10] ILKs of plants contain multiple ILK genes. Unlike animals that contain few ILK genes[10] ILKs have been found to possess oncogenic properties. ILKs control the activity of serine/threonine phosphatases.[9]