New partners and phosphorylation sites of focal adhesion kinase identified by mass spectrometry

Biochim Biophys Acta. 2016 Jul;1860(7):1388-94. doi: 10.1016/j.bbagen.2016.02.019. Epub 2016 Mar 28.


The regulation of focal adhesion kinase (FAK) involves phosphorylation and multiple interactions with other signaling proteins. Some of these pathways are relevant for nervous system functions such as branching, axonal guidance, and plasticity. In this study, we screened mouse brain to identify FAK-interactive proteins and phosphorylatable residues as a first step to address the neuronal functions of this kinase. Using mass spectrometry analysis, we identified new phosphorylated sites (Thr 952, Thr 1048, and Ser 1049), which lie in the FAT domain; and putative new partners for FAK, which include cytoskeletal proteins such as drebrin and MAP 6, adhesion regulators such as neurabin-2 and plakophilin 1, and synapse-associated proteins such as SynGAP and a NMDA receptor subunit. Our findings support the participation of brain-localized FAK in neuronal plasticity.

Keywords: Brain; Focal adhesion kinase; Mass spectrometry; Synapse.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Animals, Newborn
  • Binding Sites
  • Brain / enzymology*
  • Brain / physiopathology
  • Catalytic Domain
  • Chromatography, Liquid
  • Disease Models, Animal
  • Enzyme Activation
  • Focal Adhesion Kinase 1 / chemistry
  • Focal Adhesion Kinase 1 / metabolism*
  • Immunoprecipitation
  • Mice
  • Neuronal Plasticity
  • Pentylenetetrazole
  • Phosphorylation
  • Protein Binding
  • Seizures / enzymology*
  • Seizures / physiopathology
  • Signal Transduction
  • Tandem Mass Spectrometry*


  • Focal Adhesion Kinase 1
  • Ptk2 protein, mouse
  • Pentylenetetrazole