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

Maho Takahashi, Tara J. Dillon, Chang Liu, Yumi Kariya, Zhiping Wang, Philip J.S. Stork

Research output: Contribution to journalArticle

28 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)27712-27723
Number of pages12
JournalJournal of Biological Chemistry
Volume288
Issue number39
DOIs
StatePublished - Sep 27 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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