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• W2129130876 abstract "The C-terminus domain of G protein-coupled receptors confers a functional cytoplasmic interface involved in protein association. By screening a rat brain cDNA library using the yeast two-hybrid system with the C-terminus domain of the dopamine D(3) receptor (D(3)R) as bait, we characterized a new interaction with the PDZ domain-containing protein, GIPC (GAIP interacting protein, C terminus). This interaction was specific for the dopamine D(2) receptor (D(2)R) and D(3)R, but not for the dopamine D(4) receptor (D(4)R) subtype. Pull-down and affinity chromatography assays confirmed this interaction with recombinant and endogenous proteins. Both GIPC mRNA and protein are widely expressed in rat brain and together with the D(3)R in neurons of the islands of Calleja at plasma membranes and in vesicles. GIPC reduced D(3)R signaling, cointernalized with D(2)R and D(3)R, and sequestered receptors in sorting vesicles to prevent their lysosomal degradation. Through its dimerization, GIPC acts as a selective scaffold protein to assist receptor functions. Our results suggest a novel function for GIPC in the maintenance, trafficking, and signaling of GPCRs." @default.
• W2129130876 created "2016-06-24" @default.
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• W2129130876 date "2004-02-01" @default.
• W2129130876 modified "2023-09-24" @default.
• W2129130876 title "Interactions of GIPC with Dopamine D₂, D₃but not D₄Receptors Define a Novel Mode of Regulation of G Protein-coupled Receptors" @default.
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• W2129130876 doi "https://doi.org/10.1091/mbc.e03-05-0293" @default.
• W2129130876 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/329290" @default.
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