Phosphorylation of vitronectin by casein kinase II. Identification of the sites and their promotion of cell adhesion and spreading.

@article{Seger1998PhosphorylationOV,
  title={Phosphorylation of vitronectin by casein kinase II. Identification of the sites and their promotion of cell adhesion and spreading.},
  author={Dalia Seger and Zeev Gechtman and Shmuel Shaltiel},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 38},
  pages={24805-13}
}
The cell adhesion protein vitronectin (Vn) was previously shown to be the major target in human blood for an extracellular protein kinase A, which is released from platelets upon their physiological stimulation with thrombin and also prevails as an ectoenzyme in several other types of blood cells. Because plasma Vn was shown to have only one protein kinase A phosphorylation site (Ser378) but to contain approximately 3 mol of covalently bound phosphate, and because human serum and blood cells… CONTINUE READING

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