ILK 介导的肌动蛋白组装的特征分析。

Characterization of pseudokinase ILK-mediated actin assembly.

机构信息

Department of Cardiovascular & Metabolic Sciences, Lerner Research Institute, Cleveland Clinic, Cleveland, OH, United States.

出版信息

Methods Enzymol. 2022;667:123-146. doi: 10.1016/bs.mie.2022.03.027. Epub 2022 Apr 18.

DOI:10.1016/bs.mie.2022.03.027

PMID:35525540

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.

摘要

假激酶 ILK 是一种参与调节黏着斑组装和细胞-细胞外基质黏附的关键蛋白。通过与包含肌动蛋白结合 WH2 基序的衔接蛋白 PINCH 和 Parvin 形成紧密的三聚体复合物 (IPP)，IPP 可以促进独特的肌动蛋白束的形成，从而连接黏着斑和肌动蛋白细胞骨架，并触发细胞骨架重排和动态细胞黏附过程，如细胞铺展和迁移。本章详细描述了 IPP 介导的肌动蛋白结合和束形成的特性。