E-cadherin phosphorylation by protein kinase D1/protein kinase C{mu} is associated with altered cellular aggregation and motility in prostate cancer.

@article{Jaggi2005EcadherinPB,
  title={E-cadherin phosphorylation by protein kinase D1/protein kinase C\{mu\} is associated with altered cellular aggregation and motility in prostate cancer.},
  author={Meena Jaggi and P Syamasundar Rao and David J. Smith and Margaret J. Wheelock and Keith R. Johnson and George P. Hemstreet and Kethandapatti C. Balaji},
  journal={Cancer research},
  year={2005},
  volume={65 2},
  pages={483-92}
}
The cadherin family of transmembrane glycoproteins plays a critical role in cell-to-cell adhesion and cadherin dysregulation is strongly associated with cancer metastasis and progression. In this study, we report a novel interaction between protein kinase D1 [PKD1; formerly known as protein kinase C mu (PKCmu)] and E-cadherin. PKD1 is a serine/threonine-specific kinase known to play a role in multiple cellular processes including apoptosis, cytoskeleton remodeling, and invasion. Our study shows… CONTINUE READING

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Uncoupling of protein kinase D from suppression of EGF-dependent c-Jun PKD1 Phosphorylates E-Cadherin www.aacrjournals.org

  • C Hurd, E. Rozengurt
  • Cancer Res
  • 2005
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