Enteropathogenic Escherichia coli recruits the cellular inositol phosphatase SHIP2 to regulate actin-pedestal formation.

@article{Smith2010EnteropathogenicEC,
  title={Enteropathogenic Escherichia coli recruits the cellular inositol phosphatase SHIP2 to regulate actin-pedestal formation.},
  author={K. Aaron Smith and Daniel E Humphreys and Peter J. Hume and Vassilis Koronakis},
  journal={Cell host & microbe},
  year={2010},
  volume={7 1},
  pages={13-24}
}
Adhesion of enteropathogenic Escherichia coli to epithelial cells triggers actin-rich pedestal formation beneath the bacteria. Pedestal formation requires delivery and insertion of the bacterial translocated intimin receptor (Tir) into the host plasma membrane. The C-terminal regions in Tir, encompassing Y483 and Y511, share sequence similarity with cellular immunoreceptor tyrosine-based inhibition motifs (ITIMs), which are critical regulators of eukaryotic signaling pathways. We demonstrate… CONTINUE READING

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