Protein kinase A-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration.

@article{Takahashi2013ProteinKA,
  title={Protein kinase A-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration.},
  author={Maho Takahashi and Tara J. Dillon and Chang Liu and Yumi Kariya and Zhiping Wang and Philip J S Stork},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 39},
  pages={27712-23}
}
The small G protein Rap1 can mediate "inside-out signaling" by recruiting effectors to the plasma membrane that signal to pathways involved in cell adhesion and cell migration. This action relies on the membrane association of Rap1, which is dictated by post-translational prenylation as well as by a stretch of basic residues within its carboxyl terminus. One feature of this stretch of acidic residues is that it lies adjacent to a functional phosphorylation site for the cAMP-dependent protein… CONTINUE READING
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