Integrin-linked kinase

4HI9, 2KBX, 3F6Q, 3IXE, 3KMU, 3KMW, 3REP, 4HI8361116202ENSG00000166333ENSMUSG00000030890Q13418O55222NM_001014794NM_001014795NM_001278441NM_001278442NM_004517NM_001161724NM_010562NP_001014794NP_001014795NP_001265370NP_001265371NP_004508NP_001155196NP_034692Integrin-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 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. Animal ILKs have been linked to the pinch- parvin complex which control muscle development. Mice lacking ILK were embryonic lethal due to lack of organized muscle cell development. In mammals ILK lacks catalytic activity but supports scaffolding protein functions for focal adhesions. In plants, ILKs signal complexes to focal adhesion sites. ILKs of plants contain multiple ILK genes. Unlike animals that contain few ILK genes ILKs have been found to possess oncogenic properties. ILKs control the activity of serine/threonine phosphatases. 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), interacts with the cytoplasmic domain of beta-1 integrin. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene. Recent results showed that the C-terminal kinase domain is actually a pseudo-kinase with adaptor function. In 2008, ILK was found to localize to the centrosome and regulate mitotic spindle organization. Integrin-linked kinase has been shown to interact with: ILKs function by interacting with the many transmembrane receptors to regulate different signaling cascades. ILK1 has been found in the root system of most plants where they are co-localized on the plasma membrane and endoplasmic reticulum where they transport ions across the plasma membrane ILK1 is responsible for the control of osmotic and salt stress, control of the uptake of nutrients based on availability and pathogen detection. ILK1 is linked to hyperosmotic stress sensitivity. ILK1 reduced salt stress in seedlings placed in solution with increased concentrations of salt. ILK1 concentrations remain fairly constant throughout development regardless of a high salt exposure. Previously, it was believed that K+ accumulation was reduced in increased salt concentration. K+ homeostasis is not affected in high salt concentrations. During periods of high salt stress, K+ concentrations in the presence of ILK1 was maintained at the existing level. Potassium transport is required for flg22 root growth inhibition and potassium transport was affected by flg22. Potassium levels modulate the activation of flg22, a flagellin peptide composed of 22 amino acids that triggers pathogen-associated molecular patterns (PAMPs). PAMPs functions by activating regulators of bacterial pathogen alert system. Ion concentration levels of Mn2+, Mg2+, S and Ca2+ were also affected after PAMP regulators were mobilized.