Focal adhesion kinase signaling in unexpected places

Curr Opin Cell Biol. 2017 Apr;45:24-30. doi: 10.1016/ Epub 2017 Feb 16.


Focal adhesion kinase (FAK) is a cytoplasmic protein-tyrosine kinase first identified at extracellular matrix and integrin receptor cell adhesion sites and is a key regulator of cell movement. FAK is activated by a variety of stimuli. Herein, we discuss advances in conformational-associated FAK activation and dimerization mechanisms. Additionally, new roles have emerged for FAK signaling at cell adhesions, adherens junctions, endosomes, and the nucleus. In light of these new findings, we review how FAK activation at these sites is connected to the regulation of integrin recycling-activation, vascular permeability, cell survival, and transcriptional regulation, respectively. Studies uncovering FAK signaling connections in unexpected places within cells have yielded important new regulatory insights in cell biology.

Publication types

  • Review

MeSH terms

  • Adherens Junctions / metabolism*
  • Animals
  • Binding Sites
  • Cell Adhesion
  • Cell Movement
  • Endosomes / metabolism
  • Enzyme Activation
  • Extracellular Matrix / metabolism
  • Focal Adhesion Protein-Tyrosine Kinases / chemistry
  • Focal Adhesion Protein-Tyrosine Kinases / metabolism*
  • Humans
  • Integrins / metabolism
  • Phosphorylation
  • Signal Transduction*


  • Integrins
  • Focal Adhesion Protein-Tyrosine Kinases