Regulation of Rnd3 localization and function by protein kinase C alpha-mediated phosphorylation.

@article{Madigan2009RegulationOR,
  title={Regulation of Rnd3 localization and function by protein kinase C alpha-mediated phosphorylation.},
  author={James P. Madigan and Brian O. Bodemann and Donita C. Brady and Brian J. Dewar and Patricia J. Keller and Michael Leitges and Mark R Philips and Anne J Ridley and Channing J Der and Adrienne D. Cox},
  journal={The Biochemical journal},
  year={2009},
  volume={424 1},
  pages={153-61}
}
The Rnd proteins (Rnd1, Rnd2 and Rnd3/RhoE) form a distinct branch of the Rho family of small GTPases. Altered Rnd3 expression causes changes in cytoskeletal organization and cell cycle progression. Rnd3 functions to decrease RhoA activity, but how Rnd3 itself is regulated to cause these changes is still under investigation. Unlike other Rho family proteins, Rnd3 is regulated not by GTP/GDP cycling, but at the level of expression and by post-translational modifications such as prenylation and… CONTINUE READING
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