ILK1 Human

Integrin-linked kinase (ILK) is a multifunctional protein that plays a crucial role in cell-matrix interactions, cell adhesion, and anchorage-dependent cell growth. Initially discovered in 1996 by Hannigan and colleagues, ILK has since been recognized as a significant player in various cellular processes, including proliferation, survival, differentiation, migration, invasion, and angiogenesis .

ILK is composed of three distinct domains: an N-terminal ankyrin-repeat domain, a pleckstrin homology (PH)-like domain, and a kinase catalytic domain . Despite being initially classified as a serine/threonine-protein kinase, its catalytic activity has been questioned due to structural and functional issues, leading to its classification as a pseudokinase . However, some studies have demonstrated that ILK can function as a Mn2±dependent protein kinase, regulating the phosphorylation of various substrates .

ILK localizes primarily to focal adhesions, myofilaments, and centrosomes, where it forms distinct multi-protein complexes to regulate cell adhesion, cell contraction, actin cytoskeletal organization, and mitotic spindle assembly . It interacts with the cytoplasmic domains of beta integrins, acting as a proximal receptor kinase that regulates integrin-mediated signal transduction .

Dysfunction of ILK is associated with various diseases, including cardiomyopathies and tumorigenesis . Mutations in the ILK gene have been linked to cardiomyopathies, highlighting its importance in maintaining normal cellular functions . Additionally, ILK’s pro-oncogenic activity in tumorigenesis underscores its potential as a therapeutic target in cancer treatment .

Human recombinant ILK has been extensively studied to understand its role in cellular processes and its potential therapeutic applications. Recombinant ILK is typically expressed and purified to high homogeneity, allowing researchers to characterize its kinase activity and investigate its interactions with other proteins .