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

51 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
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

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title = "Protein kinase a-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration",

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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doi = "10.1074/jbc.M113.466904",

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journal = "Journal of Biological Chemistry",

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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.

UR - https://www.scopus.com/pages/publications/84884800622

U2 - 10.1074/jbc.M113.466904

DO - 10.1074/jbc.M113.466904

M3 - Article

C2 - 23946483

AN - SCOPUS:84884800622

SN - 0021-9258

VL - 288

SP - 27712

EP - 27723

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 39

ER -

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

Abstract

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