Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase.

@article{Delcommenne1998Phosphoinositide3OHKR,
  title={Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase.},
  author={Marc Delcommenne and Clara Wee Keat Tan and Virginia Gray and Laura Ru{\'e} and James R Woodgett and Shoukat Dedhar},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 19},
  pages={11211-6}
}
Integrin-linked kinase (ILK) is an ankyrin-repeat containing serine-threonine protein kinase capable of interacting with the cytoplasmic domains of integrin beta1, beta2, and beta3 subunits. Overexpression of ILK in epithelial cells disrupts cell-extracellular matrix as well as cell-cell interactions, suppresses suspension-induced apoptosis (also called Anoikis), and stimulates anchorage-independent cell cycle progression. In addition, ILK induces nuclear translocation of beta-catenin, where… CONTINUE READING
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Delcommenne et al

  • K. Vouri, Ruoslahti, E. Science 266, 1576–1578. 11216 Cell Biology
  • Proc. Natl. Acad. Sci. USA 95
  • 1998

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