Phosphoinositide binding and phosphorylation act sequentially in the activation mechanism of ezrin

@article{Fivet2004PhosphoinositideBA,
  title={Phosphoinositide binding and phosphorylation act sequentially in the activation mechanism of ezrin},
  author={Bruno Fi{\'e}vet and Alexis Gautreau and Christian Roy and Laurence Del Maestro and Paul H. Mangeat and Daniel Louvard and Monique Arpin},
  journal={The Journal of Cell Biology},
  year={2004},
  volume={164},
  pages={653 - 659}
}
Ezrin, a membrane-actin cytoskeleton linker, which participates in epithelial cell morphogenesis, is held inactive in the cytoplasm through an intramolecular interaction. Phosphatidylinositol 4,5-bisphosphate (PIP2) binding and the phosphorylation of threonine 567 (T567) are involved in the activation process that unmasks both membrane and actin binding sites. Here, we demonstrate that ezrin binding to PIP2, through its NH2-terminal domain, is required for T567 phosphorylation and thus for the… CONTINUE READING
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