Phosphorylation of the Par-1 polarity kinase by protein kinase D regulates 14-3-3 binding and membrane association.

@article{Watkins2008PhosphorylationOT,
  title={Phosphorylation of the Par-1 polarity kinase by protein kinase D regulates 14-3-3 binding and membrane association.},
  author={Janis L Watkins and Katherine T Lewandowski and Sarah E M Meek and Peter Storz and A. C. Toker and Helen Piwnica-Worms},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2008},
  volume={105 47},
  pages={18378-83}
}
The Par-1 protein kinases are conserved from yeast to humans, where they function as key polarity determinants. The mammalian Par-1 family is comprised of 4 members (Par-1a, -b, -c, and -d). Previously, we demonstrated that atypical protein kinase C (aPKC) phosphorylates the Par-1 kinases on a conserved threonine residue (T595) to regulate localization and kinase activity. Here, we demonstrate that Par-1b is also regulated by another arm of the PKC pathway, one that involves novel PKCs (nPKC… CONTINUE READING

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