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Research ArticleArticle

Recruitment of RGS2 and RGS4 to the Plasma Membrane by G Proteins and Receptors Reflects Functional Interactions

Anju Anne Roy, Kara E. Lemberg and Peter Chidiac
Molecular Pharmacology September 2003, 64 (3) 587-593; DOI: https://doi.org/10.1124/mol.64.3.587
Anju Anne Roy
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Kara E. Lemberg
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Peter Chidiac
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Abstract

N-terminally green fluorescent protein (GFP)-tagged regulator of G protein signaling (RGS) 2 and RGS4 fusion proteins expressed in human embryonic kidney 293 cells localized to the nucleus and cytosol, respectively. They were selectively recruited to the plasma membrane by G proteins and correspondingly by receptors that activate those G proteins: GFP-RGS2 when coexpressed with Gαs, β2-adrenergic receptor, Gαq, or AT1A angiotensin II receptor, and GFP-RGS4 when coexpressed with Gαi2 or M2 muscarinic receptor. G protein mutants with reduced RGS affinity did not produce this effect, implying that the recruitment involves direct binding to G proteins and is independent of downstream signaling events. Neither agonists nor inverse agonists altered receptor-promoted RGS association with the plasma membrane, and expressing either constitutively activated or poorly activated G protein mutants produced effects similar to those of their wild-type counterparts. Thus, intracellular interactions between these proteins seem to be relatively stable and insensitive to the activation state of the G protein, in contrast to the transient increases in RGS-G protein association known to be caused by G protein activation in solution-based assays. G protein effects on RGS localization were mirrored by RGS effects on G protein function. RGS4 was more potent than RGS2 in promoting steady-state Gi GTPase activity, whereas RGS2 inhibited Gs-dependent increases in intracellular cAMP, suggesting that G protein signaling in cells is regulated by the selective recruitment of RGS proteins to the plasma membrane.

  • Received October 15, 2002.
  • Accepted May 28, 2003.
  • The American Society for Pharmacology and Experimental Therapeutics
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Molecular Pharmacology: 64 (3)
Molecular Pharmacology
Vol. 64, Issue 3
1 Sep 2003
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Research ArticleArticle

Recruitment of RGS2 and RGS4 to the Plasma Membrane by G Proteins and Receptors Reflects Functional Interactions

Anju Anne Roy, Kara E. Lemberg and Peter Chidiac
Molecular Pharmacology September 1, 2003, 64 (3) 587-593; DOI: https://doi.org/10.1124/mol.64.3.587

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Research ArticleArticle

Recruitment of RGS2 and RGS4 to the Plasma Membrane by G Proteins and Receptors Reflects Functional Interactions

Anju Anne Roy, Kara E. Lemberg and Peter Chidiac
Molecular Pharmacology September 1, 2003, 64 (3) 587-593; DOI: https://doi.org/10.1124/mol.64.3.587
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