| Primary Identifier | IPR035692 | Type | Domain |
| Short Name | PK_ILK |
| description | The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Integrin linked kinase (ILK) contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration []. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase []. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation [, ]. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin [, ]. |
