Structural basis of focal adhesion localization of LIM-only adaptor PINCH by integrin-linked kinase.

ABSTRACT: The LIM-only adaptor PINCH (the particularly interesting cysteine- and histidine-rich protein) plays a pivotal role in the assembly of focal adhesions (FAs), supramolecular complexes that transmit mechanical and biochemical information between extracellular matrix and actin cytoskeleton, regulating diverse cell adhesive processes such as cell migration, cell spreading, and survival. A key step for the PINCH function is its localization to FAs, which depends critically on the tight binding of PINCH to integrin-linked kinase (ILK). Here we report the solution NMR structure of the core ILK.PINCH complex (28 kDa, K(D) approximately 68 nm) involving the N-terminal ankyrin repeat domain (ARD) of ILK and the first LIM domain (LIM1) of PINCH. We show that the ILK ARD exhibits five sequentially sta

SUBMITTER: Yang Y 

PROVIDER: S-EPMC2645833 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature