Protein-tyrosine kinase CAKβ/PYK2 is activated by binding Ca2+/calmodulin to FERM F2 α2 helix and thus forming its dimer

@article{Kohno2008ProteintyrosineKC,
  title={Protein-tyrosine kinase CAK$\beta$/PYK2 is activated by binding Ca2+/calmodulin to FERM F2 $\alpha$2 helix and thus forming its dimer},
  author={Takayuki Kohno and Eiko Matsuda and Hiroko Sasaki and Terukatsu Sasaki},
  journal={Biochemical Journal},
  year={2008},
  volume={410},
  pages={513-523}
}
CAKβ (cell adhesion kinase β)/PYK2 (proline-rich tyrosine kinase 2) is the second protein-tyrosine kinase of the FAK (focal adhesion kinase) subfamily. It is different from FAK in that it is activated following an increase in cytoplasmic free Ca 2+ . In the present study we have investigated how Ca 2+ activates CAKβ/PYK2. Calmodulin-agarose bound CAKβ/PYK2, but not FAK, in the presence of CaCl 2 . An α-helix (F2-α2) present in the FERM (band four-point-one, ezrin, radixin, moesin homology) F2… 

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