Characterization of pseudokinase ILK-mediated actin assembly

Abstract

Pseudokinase ILK is a key protein involved in regulating focal adhesion assembly and cell-extracellular matrix adhesion. By forming a tight trimeric complex (IPP) with adaptor proteins PINCH and Parvin that both contain an actin binding WH2 motif, IPP can promote the formation of unique actin bundles thereby linking the focal adhesions and actin cytoskeleton and triggering cytoskeleton reassembly and dynamic cell adhesion processes such as cell spreading and migration. This chapter describes detailed characterization of the IPP-mediated actin binding and bundle formation.

Keywords: Actin bundling; Cell adhesion; ILK; Integrin; Pseudokinase.