Nck-independent actin assembly is mediated by two phosphorylated tyrosines within enteropathogenic Escherichia coli Tir.

@article{Campellone2005NckindependentAA,
  title={Nck-independent actin assembly is mediated by two phosphorylated tyrosines within enteropathogenic Escherichia coli Tir.},
  author={Kenneth G Campellone and John M Leong},
  journal={Molecular microbiology},
  year={2005},
  volume={56 2},
  pages={416-32}
}
Enteropathogenic Escherichia coli (EPEC) stimulates tyrosine-kinase signalling cascades to trigger localized actin assembly within mammalian cells. During actin 'pedestal' formation, the EPEC effector protein Tir is translocated into the plasma membrane, becomes phosphorylated on tyrosine-474 (Y474) and promotes recruitment of the mammalian adaptor protein Nck to efficiently activate N-WASP-Arp2/3-mediated actin polymerization. Tir also triggers localized actin assembly in the absence of Nck… CONTINUE READING

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