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

doi:10.1074/jbc.M113.466904

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 journal › Article › peer-review

41 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 language	English (US)
Pages (from-to)	27712-27723
Number of pages	12
Journal	Journal of Biological Chemistry
Volume	288
Issue number	39
DOIs	https://doi.org/10.1074/jbc.M113.466904
State	Published - Sep 27 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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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.",

author = "Maho Takahashi and Dillon, {Tara J.} and Chang Liu and Yumi Kariya and Zhiping Wang and Stork, {Philip J.S.}",

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T1 - Protein kinase a-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration

AU - Takahashi, Maho

AU - Dillon, Tara J.

AU - Liu, Chang

AU - Kariya, Yumi

AU - Wang, Zhiping

AU - Stork, Philip J.S.

PY - 2013/9/27

Y1 - 2013/9/27

N2 - 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.

AB - 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.

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

Abstract

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