Phosphatidylinositol 5-phosphate regulates invasion through binding and activation of Tiam1.

@article{Viaud2014Phosphatidylinositol5R,
  title={Phosphatidylinositol 5-phosphate regulates invasion through binding and activation of Tiam1.},
  author={Julien Viaud and Fr{\'e}d{\'e}ric Lagarrigue and Damien Ramel and Sophie Allart and Ga{\"e}tan Chicanne and Laurie Ceccato and Delphine Courilleau and Jean-Marie Xuereb and Olivier Pertz and Bernard Payrastre and Fr{\'e}d{\'e}rique Gaits-Iacovoni},
  journal={Nature communications},
  year={2014},
  volume={5},
  pages={4080}
}
PtdIns5P is a lipid messenger acting as a stress-response mediator in the nucleus, and known to maintain cell activation through traffic alterations upon bacterial infection. Here, we show that PtdIns5P regulates actin dynamics and invasion via recruitment and activation of the exchange factor Tiam1 and Rac1. Restricted Rac1 activation results from the binding of Tiam1 DH-PH domains to PtdIns5P. Using an assay that mimics Rac1 membrane anchoring by using Rac1-His and liposomes containing Ni(2… CONTINUE READING
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