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MBC in Press, published online ahead of print September 8, 2004
Mol. Biol. Cell 10.1091/mbc.E04-04-0285

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Submitted on April 6, 2004
Revised on July 29, 2004
Accepted on August 16, 2004

GIPC Recruits GAIP (RGS19) to Attenuate Dopamine D2 Receptor Signaling

Freddy Jeanneteau,*{dagger} Olivier Guillin,* Jorge Diaz,{ddagger} Nathalie Griffon,* and Pierre Sokoloff*

*Unité de Neurobiologie et Pharmacologie Moléculaire INSERM U 573, Centre Paul Broca, 75104 Paris, France; {ddagger}Laboratoire de Physiologie, Faculté de Pharmacie, 75006 Paris, France

Monitoring Editor: Suzanne Pfeffer

Pleiotropic G proteins are essential for the action of hormones and neurotransmitters and are activated by stimulation of G protein-coupled receptors (GPCR), which initiates heterotrimer dissociation of the G protein, exchange of GDP for GTP on its G{alpha} subunit and activation of effector proteins. Regulator of G protein signaling (RGS) proteins regulate this cascade and can be recruited to the membrane upon GPCR activation. Direct functional interaction between RGS and GPCR has been hypothesized. We show that recruitment of GAIP (RGS19) by the dopamine D2 receptor (D2R), a GPCR, required the scaffold protein GIPC (GAIP-interacting protein, C terminus) and that all three were coexpressed in neurons and neuroendocrine cells. Dynamic translocation of GAIP to the plasma membrane and coassembly in a protein complex in which GIPC was a required component was dictated by D2R activation and physical interactions. In addition, two different D2R-mediated responses were regulated by the GTPase activity of GAIP at the level of the G protein coupling in a GIPC-dependent manner. Since GIPC exclusively interacted with GAIP and selectively with subsets of GPCR, this mechanism may serve to sort GPCR signaling in cells that usually express a large repertoire of GPCRs, G proteins and RGS.

{dagger}Corresponding author. E-mail: jeannet{at}broca.inserm.fr




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