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

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Abstract

Background: The small G protein Rap1 is phosphorylated within its carboxyl terminus by the cAMP-dependent protein kinase PKA. Results: This phosphorylation removes Rap1 from the plasma membrane to limit Rap1 signaling. Conclusion: Rap1 phosphorylation switches Rap1 off the membrane and terminates its activation. Significance: Carboxyl-terminal phosphorylation may be common among small G proteins to regulate GTP/GDP cycling and downstream signaling. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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Takahashi, M., Dillon, T. J., Liu, C., Kariya, Y., Wang, Z., & Stork, P. J. S. (2013). Protein kinase a-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration. Journal of Biological Chemistry, 288(39), 27712–27723. https://doi.org/10.1074/jbc.M113.466904

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