Characterization of pseudokinase ILK-mediated actin assembly
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Updated: Sep 24, 2025

Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics
Published on: August 25, 2022
1Department of Cardiovascular & Metabolic Sciences, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, United States.
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.
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