Dataset Information

Compartmentalization of protein kinase A signaling by the heterotrimeric G protein Go.

ABSTRACT: G(o), a member of the G(o/i) family, is the most abundant heterotrimeric G protein in brain. Most functions of G(o) are mediated by the G(betagamma) dimer; effector(s) for its alpha-subunit have not been clearly defined. Here we report that G(oalpha) interacts directly with cAMP-dependent protein kinase (PKA) through its GTPase domain. This interaction did not inhibit the kinase function of PKA but interfered with nuclear translocation of PKA while sparing its cytosolic function. This regulatory mechanism by which G(o) bifurcates PKA signaling may provide insights into how G(o) regulates complex processes such as neuritogenesis, synaptic plasticity, and cell transformation.

SUBMITTER: Ghil S

PROVIDER: S-EPMC1682014 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature

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Compartmentalization of protein kinase A signaling by the heterotrimeric G protein Go.

Ghil Sungho S Choi Jung-Mi JM Kim Sung-Soo SS Lee Young-Don YD Liao Yanhong Y Birnbaumer Lutz L Suh-Kim Haeyoung H

Proceedings of the National Academy of Sciences of the United States of America 20061205 50

G(o), a member of the G(o/i) family, is the most abundant heterotrimeric G protein in brain. Most functions of G(o) are mediated by the G(betagamma) dimer; effector(s) for its alpha-subunit have not been clearly defined. Here we report that G(oalpha) interacts directly with cAMP-dependent protein kinase (PKA) through its GTPase domain. This interaction did not inhibit the kinase function of PKA but interfered with nuclear translocation of PKA while sparing its cytosolic function. This regulatory ...[more]

PMID: 17148597

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Project description:BackgroundArabidopsis, 7-transmembrane Regulator of G signaling protein 1 (AtRGS1) modulates canonical G protein signaling by promoting the inactive state of heterotrimeric G protein complex on the plasma membrane. It is known that plant leucine-rich repeat receptor-like kinases (LRR RLKs) phosphorylate AtRGS1 in vitro but little is known about the in vivo interaction, molecular dynamics, or the cellular consequences of this interaction.MethodsTherefore, a subset of the known RLKs that phosphorylate AtRGS1 were selected for elucidation, namely, BAK1, BIR1, FLS2. Several microscopies for both static and dynamic protein-protein interactions were used to follow in vivo interactions between the RLKs and AtRGS1 after the presentation of the Pathogen-associated Molecular Pattern, Flagellin 22 (Flg22). These microscopies included Förster Resonance Energy Transfer, Bimolecular Fluoresence Complementation, and Cross Number and Brightness Fluorescence Correlation Spectroscopy. In addition, reactive oxygen species and calcium changes in living cells were quantitated using luminometry and R-GECO1 microscopy.ResultsThe LRR RLKs BAK1 and BIR1, interact with AtRGS1 at the plasma membrane. The RLK ligand flg22 sets BAK1 in motion toward AtRGS1 and BIR1 away, both returning to the baseline orientations by 10 minutes. The C-terminal tail of AtRGS1 is important for the interaction with BAK1 and for the tempo of the AtRGS1/BIR1 dynamics. This window of time corresponds to the flg22-induced transient production of reactive oxygen species and calcium release which are both attenuated in the rgs1 and the bak1 null mutants.ConclusionsA temporal model of these interactions is proposed. flg22 binding induces nearly instantaneous dimerization between FLS2 and BAK1. Phosphorylated BAK1 interacts with and enables AtRGS1 to move away from BIR1 and AtRGS1 becomes phosphorylated leading to its endocytosis thus leading to de-repression by permitting AtGPA1 to exchange GDP for GTP. Finally, the G protein complex becomes dissociated thus AGB1 interacts with its effector proteins leading to changes in reactive oxygen species and calcium.

Dataset Information

Compartmentalization of protein kinase A signaling by the heterotrimeric G protein Go.

Publications

Compartmentalization of protein kinase A signaling by the heterotrimeric G protein Go.

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