Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex

Bryan Serrels, Alan Serrels, Valerie G Brunton, Mark Holt, Gordon W McLean, Christopher H Gray, Gareth E Jones, Margaret C Frame

Research output: Contribution to journalArticlepeer-review


Networks of actin filaments, controlled by the Arp2/3 complex, drive membrane protrusion during cell migration. How integrins signal to the Arp2/3 complex is not well understood. Here, we show that focal adhesion kinase (FAK) and the Arp2/3 complex associate and colocalize at transient structures formed early after adhesion. Nascent lamellipodia, which originate at these structures, do not form in FAK-deficient cells, or in cells in which FAK mutants cannot be autophosphorylated after integrin engagement. The FERM domain of FAK binds directly to Arp3 and can enhance Arp2/3-dependent actin polymerization. Critically, Arp2/3 is not bound when FAK is phosphorylated on Tyr 397. Interfering peptides and FERM-domain point mutants show that FAK binding to Arp2/3 controls protrusive lamellipodia formation and cell spreading. This establishes a new function for the FAK FERM domain in forming a phosphorylation-regulated complex with Arp2/3, linking integrin signalling directly with the actin polymerization machinery.
Original languageEnglish
Pages (from-to)1046-56
Number of pages11
JournalNature Cell Biology
Issue number9
Publication statusPublished - Sep 2007


  • Actin-Related Protein 2-3 Complex
  • Actins
  • Amino Acid Sequence
  • Animals
  • Cell Adhesion
  • Cells, Cultured
  • Focal Adhesion Protein-Tyrosine Kinases
  • Integrins
  • Mice
  • Mice, Knockout
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Binding
  • Protein Structure, Tertiary
  • Pseudopodia
  • Stress Fibers
  • Tyrosine
  • Wiskott-Aldrich Syndrome Protein, Neuronal


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