The role of integrin-linked kinase in the molecular architecture of focal adhesions

Nadav Elad, Tova Volberg, Israel Patla, Vera Hirschfeld-Warneken, Carsten Grashoff, Joachim P. Spatz, Reinhard Fässler, Benjamin Geiger, Ohad Medalia

Research output: Contribution to journalArticlepeer-review

45 Scopus citations


Integrin-mediated focal adhesions (FAs) are large, multi-protein complexes that link the actin cytoskeleton to the extracellular matrix and take part in adhesion-mediated signaling. These adhesions are highly complex and diverse at the molecular level; thus, assigning particular structural or signaling functions to specific components is highly challenging. Here, we combined functional, structural and biophysical approaches to assess the role of a major FA component, namely, integrin-linked kinase (ILK), in adhesion formation. We show here that ILK plays a key role in the formation of focal complexes, early forms of integrin adhesions, and confirm its involvement in the assembly of fibronectin-bound fibrillar adhesions. Examination of ILK-null fibroblasts by cryo-electron tomography pointed to major structural changes in their FAs, manifested as disarray of the associated actin filaments and an increase in the packing density of FA-related particles. Interestingly, adhesion of the mutant cells to the substrate required a higher ligand density than in control cells. These data indicate that ILK has a key role in integrin adhesion assembly and sub-structure, and in the regulation of the FA-associated cytoskeleton.

Original languageEnglish
Pages (from-to)4099-4107
Number of pages9
JournalJournal of Cell Science
Issue number18
StatePublished - 18 Oct 2013


  • Cell adhesion
  • Correlated microscopy
  • Cryo-electron tomography
  • Focal adhesion
  • Integrin
  • Integrin-linked kinase

ASJC Scopus subject areas

  • Cell Biology


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