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 Stork

Research output: Contribution to journalArticle

25 Citations (Scopus)

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

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Phosphorylation
Protein Kinases
Cell Movement
Monomeric GTP-Binding Proteins
Membranes
Cell membranes
Cyclic AMP-Dependent Protein Kinases
Guanosine Triphosphate
Chemical activation
Switches
Cell Membrane

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Protein kinase a-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration. / Takahashi, Maho; Dillon, Tara J.; Liu, Chang; Kariya, Yumi; Wang, Zhiping; Stork, Philip.

In: Journal of Biological Chemistry, Vol. 288, No. 39, 27.09.2013, p. 27712-27723.

Research output: Contribution to journalArticle

Takahashi, Maho ; Dillon, Tara J. ; Liu, Chang ; Kariya, Yumi ; Wang, Zhiping ; Stork, Philip. / Protein kinase a-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 39. pp. 27712-27723.
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