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An interaction between the atypical angiotensin II receptor subtype AT1A and the Gq-alpha subunit of the G protein, a signaling molecule in the angiotensin II signaling pathway, was detected in HEK293 cells by reverse transcription polymerase chain reaction (RT-PCR) and confocal immunofluorescence studies. The cDNAs were amplified from total RNA of the cells using 3′ and 5′ RACE methods, cloned and expressed in COS-7 cells. The expression of a respective recombinant protein was verified by Western blotting and anti-AT1A receptor immunofluorescence in the same cells. We have shown that antibodies to specific peptides of the Gq-alpha subunit detected its location in subcellular organelles including the Golgi apparatus, ER, and plasma membrane of HEK293 cells. A specific binding of anti-AT1A receptor to the membrane fraction of the cell homogenate was further documented by immunofluorescence. This binding was competed by a specific blocking peptide and an AT1A receptor antagonist. Immunoprecipitation analysis revealed that the AT1A receptor and the Gq-alpha subunit cotrap each other. It was further shown that the putative receptor associates with the cytosolic carboxyl terminus of Gq-alpha as revealed by immunoprecipitation studies using the C-terminal GST-fusion protein. These data indicate that the AT1A receptor, by forming complexes with the cytosolic C-terminal domain of Gq-alpha, may act as a
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